MAP1LC3B: Difference between revisions

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'''Microtubule-associated proteins 1A/1B light chain 3B''' (hereafter referred to as LC3) is a [[protein]] that in humans is encoded by the ''MAP1LC3B'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP1LC3B microtubule-associated protein 1 light chain 3 beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81631| accessdate = }}</ref> LC3 is a central protein in the autophagy pathway where it functions in [[autophagy]] substrate selection and [[autophagosome]] [[biogenesis]]. LC3 is the most widely used marker of autophagosomes.<ref name name = "Klionsky_2016" />
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== Discovery ==
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LC3 was originally identified as a [[microtubule]] associated protein in rat brain.<ref>{{cite journal | vauthors = Mann SS, Hammarback JA | title = Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B | journal = The Journal of Biological Chemistry | volume = 269 | issue = 15 | pages = 11492–7 | date = April 1994 | pmid = 7908909 | doi =  | access-date =  }}</ref> However it was later found that the primary function of LC3 is in [[autophagy]], a process that involves the bulk degradation of cytoplasmic components.
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=== The ATG8 protein family ===
 
MAP1LC3B is a member of the highly conserved [[ATG8]] protein family. ATG8 proteins are present in all known [[eukaryotic]] organisms. The animal ATG8 family comprises three subfamilies: (i) microtubule-associated protein 1 light chain 3 (MAP1LC3); (ii) Golgi-associated ATPase enhancer of 16 kDa (GATE-16); and (iii) γ-amino-butyric acid receptor-associate protein (GABARAP). ''MAP1LC3B'' is one of the four genes in the MAP1LC3 subfamily (others include ''MAP1LC3A, MAP1LC3C,'' and ''MAP1LC3B2'').<ref>{{cite journal | vauthors = Shpilka T, Weidberg H, Pietrokovski S, Elazar Z | title = Atg8: an autophagy-related ubiquitin-like protein family | language = En | journal = Genome Biology | volume = 12 | issue = 7 | pages = 226 | date = July 2011 | pmid = 21867568 | pmc = 3218822 | doi = 10.1186/gb-2011-12-7-226 }}</ref>
 
==  Function ==
 
=== Cytoplasmic LC3 ===
 
Newly synthesized LC3's C-terminus is hydroylzed by a cysteine protease called [[ATG4B]] exposing Gly120, termed LC3-I.<ref>{{cite journal | vauthors = Kirisako T, Ichimura Y, Okada H, Kabeya Y, Mizushima N, Yoshimori T, Ohsumi M, Takao T, Noda T, Ohsumi Y | title = The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway | language = en | journal = The Journal of Cell Biology | volume = 151 | issue = 2 | pages = 263–76 | date = October 2000 | pmid = 11038174 | pmc = 2192639 | doi = 10.1083/jcb.151.2.263 }}</ref> LC3-I, through a series of ubiquitin-like reactions involving enzymes [[ATG7]], [[ATG3]], and [[ATG12]]-[[ATG5]]-[[ATG16L1|ATG16]], becomes conjugated to the head group of the lipid [[phosphatidylethanolamine]].<ref>{{cite journal | vauthors = Ohsumi Y | title = Molecular dissection of autophagy: two ubiquitin-like systems | journal = Nature Reviews. Molecular Cell Biology | volume = 2 | issue = 3 | pages = 211–6 | date = March 2001 | pmid = 11265251 | doi = 10.1038/35056522 }}</ref> The lipid modified form of LC3, referred to as LC3-II, is believed to be involved in autophagosome membrane expansion and fusion events.<ref>{{cite journal | vauthors = Weidberg H, Shpilka T, Shvets E, Abada A, Shimron F, Elazar Z | title = LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis | language = English | journal = Developmental Cell | volume = 20 | issue = 4 | pages = 444–54 | date = April 2011 | pmid = 21497758 | doi = 10.1016/j.devcel.2011.02.006 }}</ref> However, the exact role of LC3 in the autophagic pathway is still discussed. And the question of whether LC3 is required for autophagy is debated since knockdown of MAP1LC3B is compensated by the other members of the MAP1LC3 subfamily. Previous studies showed that MAP1LC3B knock out mice develop normally, possibly due to a then unknown compensatory mechanism.<ref>{{cite journal | vauthors = Cann GM, Guignabert C, Ying L, Deshpande N, Bekker JM, Wang L, Zhou B, Rabinovitch M | title = Developmental expression of LC3alpha and beta: absence of fibronectin or autophagy phenotype in LC3beta knockout mice | language = en | journal = Developmental Dynamics | volume = 237 | issue = 1 | pages = 187–95 | date = January 2008 | pmid = 18069693 | doi = 10.1002/dvdy.21392 }}</ref> Further work, however, demonstrated that LC3 is required for autophagy by simultaneously down-regulating all of the MAP1LC3 subfamily members.<ref>{{cite journal | vauthors = Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z | title = LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis | language = en | journal = The EMBO Journal | volume = 29 | issue = 11 | pages = 1792–802 | date = June 2010 | pmid = 20418806 | pmc = 2885923 | doi = 10.1038/emboj.2010.74 }}</ref> While yet another study argues that MAP1LC3 knockdown does to not affect bulk autophagy, whereas its [[GABARAP]] family members are crucial for the process.<ref name=":0">{{cite journal | vauthors = Szalai P, Hagen LK, Sætre F, Luhr M, Sponheim M, Øverbye A, Mills IG, Seglen PO, Engedal N | title = Autophagic bulk sequestration of cytosolic cargo is independent of LC3, but requires GABARAPs | journal = Experimental Cell Research | volume = 333 | issue = 1 | pages = 21–38 | date = April 2015 | pmid = 25684710 | doi = 10.1016/j.yexcr.2015.02.003 }}</ref><ref name=":0" /> LC3 also functions—together with autophagy receptors (e.g. [[Sequestosome 1|SQSTM1]])--in the selective capture of cargo for autophagic degradation.<ref>{{cite journal | vauthors = Johansen T, Lamark T | title = Selective autophagy mediated by autophagic adapter proteins | journal = Autophagy | volume = 7 | issue = 3 | pages = 279–96 | date = March 2011 | pmid = 21189453 | pmc = 3060413 | doi = 10.4161/auto.7.3.14487 }}</ref> Interestingly, independent of autophagosomes, a single soluble LC3 is associated with an approximately 500 kDa complex in the cytoplasm.<ref name="ReferenceA">{{cite journal | vauthors = Kraft LJ, Nguyen TA, Vogel SS, Kenworthy AK | title = Size, stoichiometry, and organization of soluble LC3-associated complexes | journal = Autophagy | volume = 10 | issue = 5 | pages = 861–77 | date = May 2014 | pmid = 24646892 | pmc = 4768459 | doi = 10.4161/auto.28175 }}</ref>
 
=== Nuclear LC3 ===
 
The importance of the nuclear functions of autophagy proteins should not be underestimated. A large pool of LC3 is present in the nucleus of a variety of different cell types.<ref>{{cite journal | vauthors = Drake KR, Kang M, Kenworthy AK | title = Nucleocytoplasmic distribution and dynamics of the autophagosome marker EGFP-LC3 | journal = PLoS One | volume = 5 | issue = 3 | pages = e9806 | date = March 2010 | pmid = 20352102 | pmc = 2843706 | doi = 10.1371/journal.pone.0009806 }}</ref> In response to starvation, nuclear LC3 is deacetylated and trafficked out of the nucleus into the cytoplasm where it functions in autophagy.<ref>{{cite journal | vauthors = Huang R, Xu Y, Wan W, Shou X, Qian J, You Z, Liu B, Chang C, Zhou T, Lippincott-Schwartz J, Liu W | title = Deacetylation of nuclear LC3 drives autophagy initiation under starvation | language = English | journal = Molecular Cell | volume = 57 | issue = 3 | pages = 456–66 | date = February 2015 | pmid = 25601754 | doi = 10.1016/j.molcel.2014.12.013 }}</ref> Nuclear LC3 interacts with [[lamin B1]], and participates in the degradation of nuclear lamina.<ref>{{cite journal | vauthors = Dou Z, Xu C, Donahue G, Shimi T, Pan JA, Zhu J, Ivanov A, Capell BC, Drake AM, Shah PP, Catanzaro JM, Ricketts MD, Lamark T, Adam SA, Marmorstein R, Zong WX, Johansen T, Goldman RD, Adams PD, Berger SL | title = Autophagy mediates degradation of nuclear lamina | journal = Nature | volume = 527 | issue = 7576 | pages = 105–9 | date = November 2015 | pmid = 26524528 | pmc = 4824414 | doi = 10.1038/nature15548 }}</ref> LC3 is also enriched in [[Nucleolus|nucleoli]] via its triple arginine motif, and associates with a number of different nuclear and nucleolar constituents including: [[MAP1B]], [[tubulin]], and several ribosomal proteins.<ref>{{cite journal | vauthors = Kraft LJ, Manral P, Dowler J, Kenworthy AK | title = Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus | language = en | journal = Traffic | volume = 17 | issue = 4 | pages = 369–99 | date = April 2016 | pmid = 26728248 | doi = 10.1111/tra.12372 }}</ref>
 
== Structure ==
 
LC3 shares structural homology with [[ubiquitin]], and thus has been termed a ubiquitin-like protein.<ref>{{cite journal | vauthors = Kouno T, Mizuguchi M, Tanida I, Ueno T, Kanematsu T, Mori Y, Shinoda H, Hirata M, Kominami E, Kawano K | title = Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains | language = en | journal = The Journal of Biological Chemistry | volume = 280 | issue = 26 | pages = 24610–7 | date = July 2005 | pmid = 15857831 | doi = 10.1074/jbc.M413565200 }}</ref> LC3 has a LDS (LIR docking site)/hydrophobic binding interface in the N terminus which interacts with LIR (LC3 Interacting Region) containing proteins.<ref name="ReferenceA"/> This domain is rich in hydrophobic amino acids, the mutation of which impairs the ability of LC3 binding with LIR containing proteins, many of which are autophagy cargo adapter proteins. For example, sequestosome (SQSTM1) interacts with Phe 52 and Leu53 aminoacids present in hydrophobic binding interface of LC3 and any mutation of these amino acids prevents LC3 interaction with SQSTM1.
 
== Post-translational regulation ==
 
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== References ==
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<ref name name = "Klionsky_2016">{{cite journal | vauthors = Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H, Acevedo Arozena A, Adachi H, Adams CM, Adams PD, Adeli K, Adhihetty PJ, Adler SG, Agam G, Agarwal R, Aghi MK, Agnello M, Agostinis P, Aguilar PV, Aguirre-Ghiso J, Airoldi EM, Ait-Si-Ali S, Akematsu T, Akporiaye ET, Al-Rubeai M, Albaiceta GM, Albanese C, Albani D, Albert ML, Aldudo J, Algül H, Alirezaei M, Alloza I, Almasan A, Almonte-Beceril M, Alnemri ES, Alonso C, Altan-Bonnet N, Altieri DC, Alvarez S, Alvarez-Erviti L, Alves S, Amadoro G, Amano A, Amantini C, Ambrosio S, Amelio I, Amer AO, Amessou M, Amon A, An Z, Anania FA, Andersen SU, Andley UP, Andreadi CK, Andrieu-Abadie N, Anel A, Ann DK, Anoopkumar-Dukie S, Antonioli M, Aoki H, Apostolova N, Aquila S, Aquilano K, Araki K, Arama E, Aranda A, Araya J, Arcaro A, Arias E, Arimoto H, Ariosa AR, Armstrong JL, Arnould T, Arsov I, Asanuma K, Askanas V, Asselin E, Atarashi R, Atherton SS, Atkin JD, Attardi LD, 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K, Isono E, Issazadeh-Navikas S, Itahana K, Itakura E, Ivanov AI, Iyer AK, Izquierdo JM, Izumi Y, Izzo V, Jäättelä M, Jaber N, Jackson DJ, Jackson WT, Jacob TG, Jacques TS, Jagannath C, Jain A, Jana NR, Jang BK, Jani A, Janji B, Jannig PR, Jansson PJ, Jean S, Jendrach M, Jeon JH, Jessen N, Jeung EB, Jia K, Jia L, Jiang H, Jiang H, Jiang L, Jiang T, Jiang X, Jiang X, Jiang X, Jiang Y, Jiang Y, Jiménez A, Jin C, Jin H, Jin L, Jin M, Jin S, Jinwal UK, Jo EK, Johansen T, Johnson DE, Johnson GV, Johnson JD, Jonasch E, Jones C, Joosten LA, Jordan J, Joseph AM, Joseph B, Joubert AM, Ju D, Ju J, Juan HF, Juenemann K, Juhász G, Jung HS, Jung JU, Jung YK, Jungbluth H, Justice MJ, Jutten B, Kaakoush NO, Kaarniranta K, Kaasik A, Kabuta T, Kaeffer B, Kågedal K, Kahana A, Kajimura S, Kakhlon O, Kalia M, Kalvakolanu DV, Kamada Y, Kambas K, Kaminskyy VO, Kampinga HH, Kandouz M, Kang C, Kang R, Kang TC, Kanki T, Kanneganti TD, Kanno H, Kanthasamy AG, Kantorow M, Kaparakis-Liaskos M, Kapuy O, Karantza V, Karim MR, Karmakar P, Kaser A, Kaushik S, Kawula T, Kaynar AM, Ke PY, Ke ZJ, Kehrl JH, Keller KE, Kemper JK, Kenworthy AK, Kepp O, Kern A, Kesari S, Kessel D, Ketteler R, Kettelhut Ido C, Khambu B, Khan MM, Khandelwal VK, Khare S, Kiang JG, Kiger AA, Kihara A, Kim AL, Kim CH, Kim DR, Kim DH, Kim EK, Kim HY, Kim HR, Kim JS, Kim JH, Kim JC, Kim JH, Kim KW, Kim MD, Kim MM, Kim PK, Kim SW, Kim SY, Kim YS, Kim Y, Kimchi A, Kimmelman AC, Kimura T, King JS, Kirkegaard K, Kirkin V, Kirshenbaum LA, Kishi S, Kitajima Y, Kitamoto K, Kitaoka Y, Kitazato K, Kley RA, Klimecki WT, Klinkenberg M, Klucken J, Knævelsrud H, Knecht E, Knuppertz L, Ko JL, Kobayashi S, Koch JC, Koechlin-Ramonatxo C, Koenig U, Koh YH, Köhler K, Kohlwein SD, Koike M, Komatsu M, Kominami E, Kong D, Kong HJ, Konstantakou EG, Kopp BT, Korcsmaros T, Korhonen L, Korolchuk VI, Koshkina NV, Kou Y, Koukourakis MI, Koumenis C, Kovács AL, Kovács T, Kovacs WJ, Koya D, Kraft C, Krainc D, Kramer H, Kravic-Stevovic T, Krek W, Kretz-Remy C, Krick R, Krishnamurthy M, Kriston-Vizi J, Kroemer G, Kruer MC, Kruger R, Ktistakis NT, Kuchitsu K, Kuhn C, Kumar AP, Kumar A, Kumar A, Kumar D, Kumar D, Kumar R, Kumar S, Kundu M, Kung HJ, Kuno A, Kuo SH, Kuret J, Kurz T, Kwok T, Kwon TK, Kwon YT, Kyrmizi I, La Spada AR, Lafont F, Lahm T, Lakkaraju A, Lam T, Lamark T, Lancel S, Landowski TH, Lane DJ, Lane JD, Lanzi C, Lapaquette P, Lapierre LR, Laporte J, Laukkarinen J, Laurie GW, Lavandero S, Lavie L, LaVoie MJ, Law BY, Law HK, Law KB, Layfield R, Lazo PA, Le Cam L, Le Roch KG, Le Stunff H, Leardkamolkarn V, Lecuit M, Lee BH, Lee CH, Lee EF, Lee GM, Lee HJ, Lee H, Lee JK, Lee J, Lee JH, Lee JH, Lee M, Lee MS, Lee PJ, Lee SW, Lee SJ, Lee SJ, Lee SY, Lee SH, Lee SS, Lee SJ, Lee S, Lee YR, Lee YJ, Lee YH, Leeuwenburgh C, Lefort S, Legouis R, Lei J, Lei QY, Leib DA, Leibowitz G, Lekli I, Lemaire SD, Lemasters JJ, Lemberg MK, Lemoine A, Leng S, Lenz G, Lenzi P, Lerman LO, Lettieri Barbato D, Leu JI, Leung HY, Levine B, Lewis PA, Lezoualc'h F, Li C, Li F, Li FJ, Li J, Li K, Li L, Li M, Li M, Li Q, Li R, Li S, Li W, Li W, Li X, Li Y, Lian J, Liang C, Liang Q, Liao Y, Liberal J, Liberski PP, Lie P, Lieberman AP, Lim HJ, Lim KL, Lim K, Lima RT, Lin CS, Lin CF, Lin F, Lin F, Lin FC, Lin K, Lin KH, Lin PH, Lin T, Lin WW, Lin YS, Lin Y, Linden R, Lindholm D, Lindqvist LM, Lingor P, Linkermann A, Liotta LA, Lipinski MM, Lira VA, Lisanti MP, Liton PB, Liu B, Liu C, Liu CF, Liu F, Liu HJ, Liu J, Liu JJ, Liu JL, Liu K, Liu L, Liu L, Liu Q, Liu RY, Liu S, Liu S, Liu W, Liu XD, Liu X, Liu XH, Liu X, Liu X, Liu X, Liu Y, Liu Y, Liu Z, Liu Z, Liuzzi JP, Lizard G, Ljujic M, Lodhi IJ, Logue SE, Lokeshwar BL, Long YC, Lonial S, Loos B, López-Otín C, López-Vicario C, Lorente M, Lorenzi PL, Lõrincz P, Los M, Lotze MT, Lovat PE, Lu B, Lu B, Lu J, Lu Q, Lu SM, Lu S, Lu Y, Luciano F, Luckhart S, Lucocq JM, Ludovico P, Lugea A, Lukacs NW, Lum JJ, Lund AH, Luo H, Luo J, Luo S, Luparello C, Lyons T, Ma J, Ma Y, Ma Y, Ma Z, Machado J, Machado-Santelli GM, Macian F, MacIntosh GC, MacKeigan JP, Macleod KF, MacMicking JD, MacMillan-Crow LA, Madeo F, Madesh M, Madrigal-Matute J, Maeda A, Maeda T, Maegawa G, Maellaro E, Maes H, Magariños M, Maiese K, Maiti TK, Maiuri L, Maiuri MC, Maki CG, Malli R, Malorni W, Maloyan A, Mami-Chouaib F, Man N, Mancias JD, Mandelkow EM, Mandell MA, Manfredi AA, Manié SN, Manzoni C, Mao K, Mao Z, Mao ZW, Marambaud P, Marconi AM, Marelja Z, Marfe G, Margeta M, Margittai E, Mari M, Mariani FV, Marin C, Marinelli S, Mariño G, Markovic I, Marquez R, Martelli AM, Martens S, Martin KR, Martin SJ, Martin S, Martin-Acebes MA, Martín-Sanz P, Martinand-Mari C, Martinet W, Martinez J, Martinez-Lopez N, Martinez-Outschoorn U, Martínez-Velázquez M, Martinez-Vicente M, Martins WK, Mashima H, Mastrianni JA, Matarese G, Matarrese P, Mateo R, Matoba S, Matsumoto N, Matsushita T, Matsuura A, Matsuzawa T, Mattson MP, Matus S, Maugeri N, Mauvezin C, Mayer A, Maysinger D, Mazzolini GD, McBrayer MK, McCall K, McCormick C, McInerney GM, McIver SC, McKenna S, McMahon JJ, McNeish IA, Mechta-Grigoriou F, Medema JP, Medina DL, Megyeri K, Mehrpour M, Mehta JL, Mei Y, Meier UC, Meijer AJ, Meléndez A, Melino G, Melino S, de Melo EJ, Mena MA, Meneghini MD, Menendez JA, Menezes R, Meng L, Meng LH, Meng S, Menghini R, Menko AS, Menna-Barreto RF, Menon MB, Meraz-Ríos MA, Merla G, Merlini L, Merlot AM, Meryk A, Meschini S, Meyer JN, Mi MT, Miao CY, Micale L, Michaeli S, Michiels C, Migliaccio AR, Mihailidou AS, Mijaljica D, Mikoshiba K, Milan E, Miller-Fleming L, Mills GB, Mills IG, Minakaki G, Minassian BA, Ming XF, Minibayeva F, Minina EA, Mintern JD, Minucci S, Miranda-Vizuete A, Mitchell CH, Miyamoto S, Miyazawa K, Mizushima N, Mnich K, Mograbi B, Mohseni S, Moita LF, Molinari M, Molinari M, Møller AB, Mollereau B, Mollinedo F, Mongillo M, Monick MM, Montagnaro S, Montell C, Moore DJ, Moore MN, Mora-Rodriguez R, Moreira PI, Morel E, Morelli MB, Moreno S, Morgan MJ, Moris A, Moriyasu Y, Morrison JL, Morrison LA, Morselli E, Moscat J, Moseley PL, Mostowy S, Motori E, Mottet D, Mottram JC, Moussa CE, Mpakou VE, Mukhtar H, Mulcahy Levy JM, Muller S, Muñoz-Moreno R, Muñoz-Pinedo C, Münz C, Murphy ME, Murray JT, Murthy A, Mysorekar IU, Nabi IR, Nabissi M, Nader GA, Nagahara Y, Nagai Y, Nagata K, Nagelkerke A, Nagy P, Naidu SR, Nair S, Nakano H, Nakatogawa H, Nanjundan M, Napolitano G, Naqvi NI, Nardacci R, Narendra DP, Narita M, Nascimbeni AC, Natarajan R, Navegantes LC, Nawrocki ST, Nazarko TY, Nazarko VY, Neill T, Neri LM, Netea MG, Netea-Maier RT, Neves BM, Ney PA, Nezis IP, Nguyen HT, Nguyen HP, Nicot AS, Nilsen H, Nilsson P, Nishimura M, Nishino I, Niso-Santano M, Niu H, Nixon RA, Njar VC, Noda T, Noegel AA, Nolte EM, Norberg E, Norga KK, Noureini SK, Notomi S, Notterpek L, Nowikovsky K, Nukina N, Nürnberger T, O'Donnell VB, O'Donovan T, O'Dwyer PJ, Oehme I, Oeste CL, Ogawa M, Ogretmen B, Ogura Y, Oh YJ, Ohmuraya M, Ohshima T, Ojha R, Okamoto K, Okazaki T, Oliver FJ, Ollinger K, Olsson S, Orban DP, Ordonez P, Orhon I, Orosz L, O'Rourke EJ, Orozco H, Ortega AL, Ortona E, Osellame LD, Oshima J, Oshima S, Osiewacz HD, Otomo T, Otsu K, Ou JH, Outeiro TF, Ouyang DY, Ouyang H, Overholtzer M, Ozbun MA, Ozdinler PH, Ozpolat B, Pacelli C, Paganetti P, Page G, Pages G, Pagnini U, Pajak B, Pak SC, Pakos-Zebrucka K, Pakpour N, Palková Z, Palladino F, Pallauf K, Pallet N, Palmieri M, Paludan SR, Palumbo C, Palumbo S, Pampliega O, Pan H, Pan W, Panaretakis T, Pandey A, Pantazopoulou A, Papackova Z, Papademetrio DL, Papassideri I, Papini A, Parajuli N, Pardo J, Parekh VV, Parenti G, Park JI, Park J, Park OK, Parker R, Parlato R, Parys JB, Parzych KR, Pasquet JM, Pasquier B, Pasumarthi KB, Patschan D, Patterson C, Pattingre S, Pattison S, Pause A, Pavenstädt H, Pavone F, Pedrozo Z, Peña FJ, Peñalva MA, Pende M, Peng J, Penna F, Penninger JM, Pensalfini A, Pepe S, Pereira GJ, Pereira PC, Pérez-de la Cruz V, Pérez-Pérez ME, Pérez-Rodríguez D, Pérez-Sala D, Perier C, Perl A, Perlmutter DH, Perrotta I, Pervaiz S, Pesonen M, Pessin JE, Peters GJ, Petersen M, Petrache I, Petrof BJ, Petrovski G, Phang JM, Piacentini M, Pierdominici M, Pierre P, Pierrefite-Carle V, Pietrocola F, Pimentel-Muiños FX, Pinar M, Pineda B, Pinkas-Kramarski R, Pinti M, Pinton P, Piperdi B, Piret JM, Platanias LC, Platta HW, Plowey ED, Pöggeler S, Poirot M, Polčic P, Poletti A, Poon AH, Popelka H, Popova B, Poprawa I, Poulose SM, Poulton J, Powers SK, Powers T, Pozuelo-Rubio M, Prak K, Prange R, Prescott M, Priault M, Prince S, Proia RL, Proikas-Cezanne T, Prokisch H, Promponas VJ, Przyklenk K, Puertollano R, Pugazhenthi S, Puglielli L, Pujol A, Puyal J, Pyeon D, Qi X, Qian WB, Qin ZH, Qiu Y, Qu Z, Quadrilatero J, Quinn F, Raben N, Rabinowich H, Radogna F, Ragusa MJ, Rahmani M, Raina K, Ramanadham S, Ramesh R, Rami A, Randall-Demllo S, Randow F, Rao H, Rao VA, Rasmussen BB, Rasse TM, Ratovitski EA, Rautou PE, Ray SK, Razani B, Reed BH, Reggiori F, Rehm M, Reichert AS, Rein T, Reiner DJ, Reits E, Ren J, Ren X, Renna M, Reusch JE, Revuelta JL, Reyes L, Rezaie AR, Richards RI, Richardson DR, Richetta C, Riehle MA, Rihn BH, Rikihisa Y, Riley BE, Rimbach G, Rippo MR, Ritis K, Rizzi F, Rizzo E, Roach PJ, Robbins J, Roberge M, Roca G, Roccheri MC, Rocha S, Rodrigues CM, Rodríguez CI, de Cordoba SR, Rodriguez-Muela N, Roelofs J, Rogov VV, Rohn TT, Rohrer B, Romanelli D, Romani L, Romano PS, Roncero MI, Rosa JL, Rosello A, Rosen KV, Rosenstiel P, Rost-Roszkowska M, Roth KA, Roué G, Rouis M, Rouschop KM, Ruan DT, Ruano D, Rubinsztein DC, Rucker EB, Rudich A, Rudolf E, Rudolf R, Ruegg MA, Ruiz-Roldan C, Ruparelia AA, Rusmini P, Russ DW, Russo GL, Russo G, Russo R, Rusten TE, Ryabovol V, Ryan KM, Ryter SW, Sabatini DM, Sacher M, Sachse C, Sack MN, Sadoshima J, Saftig P, Sagi-Eisenberg R, Sahni S, Saikumar P, Saito T, Saitoh T, Sakakura K, Sakoh-Nakatogawa M, Sakuraba Y, Salazar-Roa M, Salomoni P, Saluja AK, Salvaterra PM, Salvioli R, Samali A, Sanchez AM, Sánchez-Alcázar JA, Sanchez-Prieto R, Sandri M, Sanjuan MA, Santaguida S, Santambrogio L, Santoni G, Dos Santos CN, Saran S, Sardiello M, Sargent G, Sarkar P, Sarkar S, Sarrias MR, Sarwal MM, Sasakawa C, Sasaki M, Sass M, Sato K, Sato M, Satriano J, Savaraj N, Saveljeva S, Schaefer L, Schaible UE, Scharl M, Schatzl HM, Schekman R, Scheper W, Schiavi A, Schipper HM, Schmeisser H, Schmidt J, Schmitz I, Schneider BE, Schneider EM, Schneider JL, Schon EA, Schönenberger MJ, Schönthal AH, Schorderet DF, Schröder B, Schuck S, Schulze RJ, Schwarten M, Schwarz TL, Sciarretta S, Scotto K, Scovassi AI, Screaton RA, Screen M, Seca H, Sedej S, Segatori L, Segev N, Seglen PO, Seguí-Simarro JM, Segura-Aguilar J, Seki E, Sell C, Seiliez I, Semenkovich CF, Semenza GL, Sen U, Serra AL, Serrano-Puebla A, Sesaki H, Setoguchi T, Settembre C, Shacka JJ, Shajahan-Haq AN, Shapiro IM, Sharma S, She H, Shen CK, Shen CC, Shen HM, Shen S, Shen W, Sheng R, Sheng X, Sheng ZH, Shepherd TG, Shi J, Shi Q, Shi Q, Shi Y, Shibutani S, Shibuya K, Shidoji Y, Shieh JJ, Shih CM, Shimada Y, Shimizu S, Shin DW, Shinohara ML, Shintani M, Shintani T, Shioi T, Shirabe K, Shiri-Sverdlov R, Shirihai O, Shore GC, Shu CW, Shukla D, Sibirny AA, Sica V, Sigurdson CJ, Sigurdsson EM, Sijwali PS, Sikorska B, Silveira WA, Silvente-Poirot S, Silverman GA, Simak J, Simmet T, Simon AK, Simon HU, Simone C, Simons M, Simonsen A, Singh R, Singh SV, Singh SK, Sinha D, Sinha S, Sinicrope FA, Sirko A, Sirohi K, Sishi BJ, Sittler A, Siu PM, Sivridis E, Skwarska A, Slack R, Slaninová I, Slavov N, Smaili SS, Smalley KS, Smith DR, Soenen SJ, Soleimanpour SA, Solhaug A, Somasundaram K, Son JH, Sonawane A, Song C, Song F, Song HK, Song JX, Song W, Soo KY, Sood AK, Soong TW, Soontornniyomkij V, Sorice M, Sotgia F, Soto-Pantoja DR, Sotthibundhu A, Sousa MJ, Spaink HP, Span PN, Spang A, Sparks JD, Speck PG, Spector SA, Spies CD, Springer W, Clair DS, Stacchiotti A, Staels B, Stang MT, Starczynowski DT, Starokadomskyy P, Steegborn C, Steele JW, Stefanis L, Steffan J, Stellrecht CM, Stenmark H, Stepkowski TM, Stern ST, Stevens C, Stockwell BR, Stoka V, Storchova Z, Stork B, Stratoulias V, Stravopodis DJ, Strnad P, Strohecker AM, Ström AL, Stromhaug P, Stulik J, Su YX, Su Z, Subauste CS, Subramaniam S, Sue CM, Suh SW, Sui X, Sukseree S, Sulzer D, Sun FL, Sun J, Sun J, Sun SY, Sun Y, Sun Y, Sun Y, Sundaramoorthy V, Sung J, Suzuki H, Suzuki K, Suzuki N, Suzuki T, Suzuki YJ, Swanson MS, Swanton C, Swärd K, Swarup G, Sweeney ST, Sylvester PW, Szatmari Z, Szegezdi E, Szlosarek PW, Taegtmeyer H, Tafani M, Taillebourg E, Tait SW, Takacs-Vellai K, Takahashi Y, Takáts S, Takemura G, Takigawa N, Talbot NJ, Tamagno E, Tamburini J, Tan CP, Tan L, Tan ML, Tan M, Tan YJ, Tanaka K, Tanaka M, Tang D, Tang D, Tang G, Tanida I, Tanji K, Tannous BA, Tapia JA, Tasset-Cuevas I, Tatar M, Tavassoly I, Tavernarakis N, Taylor A, Taylor GS, Taylor GA, Taylor JP, Taylor MJ, Tchetina EV, Tee AR, Teixeira-Clerc F, Telang S, Tencomnao T, Teng BB, Teng RJ, Terro F, Tettamanti G, Theiss AL, Theron AE, Thomas KJ, Thomé MP, Thomes PG, Thorburn A, Thorner J, Thum T, Thumm M, Thurston TL, Tian L, Till A, Ting JP, Titorenko VI, Toker L, Toldo S, Tooze SA, Topisirovic I, Torgersen ML, Torosantucci L, Torriglia A, Torrisi MR, Tournier C, Towns R, Trajkovic V, Travassos LH, Triola G, Tripathi DN, Trisciuoglio D, Troncoso R, Trougakos IP, Truttmann AC, Tsai KJ, Tschan MP, Tseng YH, Tsukuba T, Tsung A, Tsvetkov AS, Tu S, Tuan HY, Tucci M, Tumbarello DA, Turk B, Turk V, Turner RF, Tveita AA, Tyagi SC, Ubukata M, Uchiyama Y, Udelnow A, Ueno T, Umekawa M, Umemiya-Shirafuji R, Underwood BR, Ungermann C, Ureshino RP, Ushioda R, Uversky VN, Uzcátegui NL, Vaccari T, Vaccaro MI, Váchová L, Vakifahmetoglu-Norberg H, Valdor R, Valente EM, Vallette F, Valverde AM, Van den Berghe G, Van Den Bosch L, van den Brink GR, van der Goot FG, van der Klei IJ, van der Laan LJ, van Doorn WG, van Egmond M, van Golen KL, Van Kaer L, van Lookeren Campagne M, Vandenabeele P, Vandenberghe W, Vanhorebeek I, Varela-Nieto I, Vasconcelos MH, Vasko R, Vavvas DG, Vega-Naredo I, Velasco G, Velentzas AD, Velentzas PD, Vellai T, Vellenga E, Vendelbo MH, Venkatachalam K, Ventura N, Ventura S, Veras PS, Verdier M, Vertessy BG, Viale A, Vidal M, Vieira HL, Vierstra RD, Vigneswaran N, Vij N, Vila M, Villar M, Villar VH, Villarroya J, Vindis C, Viola G, Viscomi MT, Vitale G, Vogl DT, Voitsekhovskaja OV, von Haefen C, von Schwarzenberg K, Voth DE, Vouret-Craviari V, Vuori K, Vyas JM, Waeber C, Walker CL, Walker MJ, Walter J, Wan L, Wan X, Wang B, Wang C, Wang CY, Wang C, Wang C, Wang C, Wang D, Wang F, Wang F, Wang G, Wang HJ, Wang H, Wang HG, Wang H, Wang HD, Wang J, Wang J, Wang M, Wang MQ, Wang PY, Wang P, Wang RC, Wang S, Wang TF, Wang X, Wang XJ, Wang XW, Wang X, Wang X, Wang Y, Wang Y, Wang Y, Wang YJ, Wang Y, Wang Y, Wang YT, Wang Y, Wang ZN, Wappner P, Ward C, Ward DM, Warnes G, Watada H, Watanabe Y, Watase K, Weaver TE, Weekes CD, Wei J, Weide T, Weihl CC, Weindl G, Weis SN, Wen L, Wen X, Wen Y, Westermann B, Weyand CM, White AR, White E, Whitton JL, Whitworth AJ, Wiels J, Wild F, Wildenberg ME, Wileman T, Wilkinson DS, Wilkinson S, Willbold D, Williams C, Williams K, Williamson PR, Winklhofer KF, Witkin SS, Wohlgemuth SE, Wollert T, Wolvetang EJ, Wong E, Wong GW, Wong RW, Wong VK, Woodcock EA, Wright KL, Wu C, Wu D, Wu GS, Wu J, Wu J, Wu M, Wu M, Wu S, Wu WK, Wu Y, Wu Z, Xavier CP, Xavier RJ, Xia GX, Xia T, Xia W, Xia Y, Xiao H, Xiao J, Xiao S, Xiao W, Xie CM, Xie Z, Xie Z, Xilouri M, Xiong Y, Xu C, Xu C, Xu F, Xu H, Xu H, Xu J, Xu J, Xu J, Xu L, Xu X, Xu Y, Xu Y, Xu ZX, Xu Z, Xue Y, Yamada T, Yamamoto A, Yamanaka K, Yamashina S, Yamashiro S, Yan B, Yan B, Yan X, Yan Z, Yanagi Y, Yang DS, Yang JM, Yang L, Yang M, Yang PM, Yang P, Yang Q, Yang W, Yang WY, Yang X, Yang Y, Yang Y, Yang Z, Yang Z, Yao MC, Yao PJ, Yao X, Yao Z, Yao Z, Yasui LS, Ye M, Yedvobnick B, Yeganeh B, Yeh ES, Yeyati PL, Yi F, Yi L, Yin XM, Yip CK, Yoo YM, Yoo YH, Yoon SY, Yoshida K, Yoshimori T, Young KH, Yu H, Yu JJ, Yu JT, Yu J, Yu L, Yu WH, Yu XF, Yu Z, Yuan J, Yuan ZM, Yue BY, Yue J, Yue Z, Zacks DN, Zacksenhaus E, Zaffaroni N, Zaglia T, Zakeri Z, Zecchini V, Zeng J, Zeng M, Zeng Q, Zervos AS, Zhang DD, Zhang F, Zhang G, Zhang GC, Zhang H, Zhang H, Zhang H, Zhang H, Zhang J, Zhang J, Zhang J, Zhang J, Zhang JP, Zhang L, Zhang L, Zhang L, Zhang L, Zhang MY, Zhang X, Zhang XD, Zhang Y, Zhang Y, Zhang Y, Zhang Y, Zhang Y, Zhao M, Zhao WL, Zhao X, Zhao YG, Zhao Y, Zhao Y, Zhao YX, Zhao Z, Zhao ZJ, Zheng D, Zheng XL, Zheng X, Zhivotovsky B, Zhong Q, Zhou GZ, Zhou G, Zhou H, Zhou SF, Zhou XJ, Zhu H, Zhu H, Zhu WG, Zhu W, Zhu XF, Zhu Y, Zhuang SM, Zhuang X, Ziparo E, Zois CE, Zoladek T, Zong WX, Zorzano A, Zughaier SM | display-authors = 6 | title = Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) | journal = Autophagy | volume = 12 | issue = 1 | pages = 1–222 | date = Jan 2016 | pmid = 26799652 | doi = 10.1080/15548627.2015.1100356 }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_MAP1LC3B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ugm.
| PDB = {{PDB2|1ugm}}, {{PDB2|1v49}}, {{PDB2|2z0d}}, {{PDB2|2z0e}}
| Name = Microtubule-associated protein 1 light chain 3 beta
| HGNCid = 13352
| Symbol = MAP1LC3B
| AltSymbols =; MAP1A/1BLC3
| OMIM = 
| ECnumber = 
| Homologene = 69359
| MGIid = 1914693
| GeneAtlas_image1 = PBB_GE_MAP1LC3B_208785_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAP1LC3B_208786_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005776 |text = autophagic vacuole}} {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0031090 |text = organelle membrane}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006914 |text = autophagy}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 81631
    | Hs_Ensembl = ENSG00000140941
    | Hs_RefseqProtein = NP_073729
    | Hs_RefseqmRNA = NM_022818
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 85982907
    | Hs_GenLoc_end = 85995883
    | Hs_Uniprot = Q9GZQ8
    | Mm_EntrezGene = 67443
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_026160
    | Mm_RefseqProtein = NP_080436
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr =
    | Mm_GenLoc_start =
    | Mm_GenLoc_end =
    | Mm_Uniprot =
  }}
}}
'''Microtubule-associated protein 1 light chain 3 beta''', also known as '''MAP1LC3B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP1LC3B microtubule-associated protein 1 light chain 3 beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81631| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product of this gene is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. Studies on the rat homolog implicate a role for this gene in autophagy, a process that involves the bulk degradation of cytoplasmic component.<ref name="entrez">{{cite web | title = Entrez Gene: MAP1LC3B microtubule-associated protein 1 light chain 3 beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81631| accessdate = }}</ref>
}}
}}


==References==
== Further reading ==
{{reflist|2}}
{{refbegin|33em}}
==Further reading==
* {{cite journal | vauthors = Kraft LJ, Kenworthy AK | title = Imaging protein complex formation in the autophagy pathway: analysis of the interaction of LC3 and Atg4B(C74A) in live cells using Förster resonance energy transfer and fluorescence recovery after photobleaching | journal = Journal of Biomedical Optics | volume = 17 | issue = 1 | pages = 011008 | date = January 2012 | pmid = 22352642 | pmc = 3380812 | doi = 10.1117/1.JBO.17.1.011008 }}
{{refbegin | 2}}
* {{cite journal | vauthors = Behrends C, Sowa ME, Gygi SP, Harper JW | title = Network organization of the human autophagy system | journal = Nature | volume = 466 | issue = 7302 | pages = 68–76 | date = July 2010 | pmid = 20562859 | pmc = 2901998 | doi = 10.1038/nature09204 }}
{{PBB_Further_reading
* {{cite journal | vauthors = Tanida I, Ueno T, Kominami E | title = LC3 conjugation system in mammalian autophagy | journal = The International Journal of Biochemistry & Cell Biology | volume = 36 | issue = 12 | pages = 2503–18 | date = December 2004 | pmid = 15325588 | doi = 10.1016/j.biocel.2004.05.009 }}
| citations =
* {{cite journal | vauthors = Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, Kominami E, Ohsumi Y, Yoshimori T | title = LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing | journal = The EMBO Journal | volume = 19 | issue = 21 | pages = 5720–8 | date = November 2000 | pmid = 11060023 | pmc = 305793 | doi = 10.1093/emboj/19.21.5720 }}
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
* {{cite journal | vauthors = Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E | title = Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p | journal = The Journal of Biological Chemistry | volume = 277 | issue = 16 | pages = 13739–44 | date = April 2002 | pmid = 11825910 | doi = 10.1074/jbc.M200385200 }}
*{{cite journal | author=Tanida I, Ueno T, Kominami E |title=LC3 conjugation system in mammalian autophagy. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 12 |pages= 2503-18 |year= 2005 |pmid= 15325588 |doi= 10.1016/j.biocel.2004.05.009 }}
* {{cite journal | vauthors = Tanida I, Tanida-Miyake E, Nishitani T, Komatsu M, Yamazaki H, Ueno T, Kominami E | title = Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs | journal = Biochemical and Biophysical Research Communications | volume = 292 | issue = 1 | pages = 256–62 | date = March 2002 | pmid = 11890701 | doi = 10.1006/bbrc.2002.6645 }}
*{{cite journal | author=Wallin M, Deinum J, Goobar L, Danielson UH |title=Proteolytic cleavage of microtubule-associated proteins by retroviral proteinases. |journal=J. Gen. Virol. |volume=71 ( Pt 9) |issue= |pages= 1985-91 |year= 1990 |pmid= 2212989 |doi= }}
* {{cite journal | vauthors = He H, Dang Y, Dai F, Guo Z, Wu J, She X, Pei Y, Chen Y, Ling W, Wu C, Zhao S, Liu JO, Yu L | title = Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B | journal = The Journal of Biological Chemistry | volume = 278 | issue = 31 | pages = 29278–87 | date = August 2003 | pmid = 12740394 | doi = 10.1074/jbc.M303800200 }}
*{{cite journal | author=Kabeya Y, Mizushima N, Ueno T, ''et al.'' |title=LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. |journal=EMBO J. |volume=19 |issue= 21 |pages= 5720-8 |year= 2000 |pmid= 11060023 |doi= 10.1093/emboj/19.21.5720 }}
* {{cite journal | vauthors = Tanida I, Sou YS, Ezaki J, Minematsu-Ikeguchi N, Ueno T, Kominami E | title = HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates | journal = The Journal of Biological Chemistry | volume = 279 | issue = 35 | pages = 36268–76 | date = August 2004 | pmid = 15187094 | doi = 10.1074/jbc.M401461200 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
* {{cite journal | vauthors = Tanida I, Ueno T, Kominami E | title = Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to expose Gly120 for lipidation and targeting to autophagosomal membranes | journal = The Journal of Biological Chemistry | volume = 279 | issue = 46 | pages = 47704–10 | date = November 2004 | pmid = 15355958 | doi = 10.1074/jbc.M407016200 }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | author=Tanida I, Tanida-Miyake E, Komatsu M, ''et al.'' |title=Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13739-44 |year= 2002 |pmid= 11825910 |doi= 10.1074/jbc.M200385200 }}
*{{cite journal | author=Tanida I, Tanida-Miyake E, Nishitani T, ''et al.'' |title=Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs. |journal=Biochem. Biophys. Res. Commun. |volume=292 |issue= 1 |pages= 256-62 |year= 2002 |pmid= 11890701 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=He H, Dang Y, Dai F, ''et al.'' |title=Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 29278-87 |year= 2003 |pmid= 12740394 |doi= 10.1074/jbc.M303800200 }}
*{{cite journal | author=Difilippantonio S, Chen Y, Pietas A, ''et al.'' |title=Gene expression profiles in human non-small and small-cell lung cancers. |journal=Eur. J. Cancer |volume=39 |issue= 13 |pages= 1936-47 |year= 2003 |pmid= 12932674 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Yang YS, Song HD, Peng YD, ''et al.'' |title=The gene expression profiling of sporadic pheochromocytoma and novel full-length cDNAs cloning. |journal=Endocr. Relat. Cancer |volume=10 |issue= 4 |pages= 621-7 |year= 2004 |pmid= 14713272 |doi=  }}
*{{cite journal  | author=Tanida I, Sou YS, Ezaki J, ''et al.'' |title=HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. |journal=J. Biol. Chem. |volume=279 |issue= 35 |pages= 36268-76 |year= 2004 |pmid= 15187094 |doi= 10.1074/jbc.M401461200 }}
*{{cite journal | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
*{{cite journal  | author=Tanida I, Ueno T, Kominami E |title=Human light chain 3/MAP1LC3B is cleaved at its carboxyl-terminal Met121 to expose Gly120 for lipidation and targeting to autophagosomal membranes. |journal=J. Biol. Chem. |volume=279 |issue= 46 |pages= 47704-10 |year= 2005 |pmid= 15355958 |doi= 10.1074/jbc.M407016200 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=81631}}
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Revision as of 02:06, 27 October 2017

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Microtubule-associated proteins 1A/1B light chain 3B (hereafter referred to as LC3) is a protein that in humans is encoded by the MAP1LC3B gene.[1] LC3 is a central protein in the autophagy pathway where it functions in autophagy substrate selection and autophagosome biogenesis. LC3 is the most widely used marker of autophagosomes.[2]

Discovery

LC3 was originally identified as a microtubule associated protein in rat brain.[3] However it was later found that the primary function of LC3 is in autophagy, a process that involves the bulk degradation of cytoplasmic components.

The ATG8 protein family

MAP1LC3B is a member of the highly conserved ATG8 protein family. ATG8 proteins are present in all known eukaryotic organisms. The animal ATG8 family comprises three subfamilies: (i) microtubule-associated protein 1 light chain 3 (MAP1LC3); (ii) Golgi-associated ATPase enhancer of 16 kDa (GATE-16); and (iii) γ-amino-butyric acid receptor-associate protein (GABARAP). MAP1LC3B is one of the four genes in the MAP1LC3 subfamily (others include MAP1LC3A, MAP1LC3C, and MAP1LC3B2).[4]

Function

Cytoplasmic LC3

Newly synthesized LC3's C-terminus is hydroylzed by a cysteine protease called ATG4B exposing Gly120, termed LC3-I.[5] LC3-I, through a series of ubiquitin-like reactions involving enzymes ATG7, ATG3, and ATG12-ATG5-ATG16, becomes conjugated to the head group of the lipid phosphatidylethanolamine.[6] The lipid modified form of LC3, referred to as LC3-II, is believed to be involved in autophagosome membrane expansion and fusion events.[7] However, the exact role of LC3 in the autophagic pathway is still discussed. And the question of whether LC3 is required for autophagy is debated since knockdown of MAP1LC3B is compensated by the other members of the MAP1LC3 subfamily. Previous studies showed that MAP1LC3B knock out mice develop normally, possibly due to a then unknown compensatory mechanism.[8] Further work, however, demonstrated that LC3 is required for autophagy by simultaneously down-regulating all of the MAP1LC3 subfamily members.[9] While yet another study argues that MAP1LC3 knockdown does to not affect bulk autophagy, whereas its GABARAP family members are crucial for the process.[10][10] LC3 also functions—together with autophagy receptors (e.g. SQSTM1)--in the selective capture of cargo for autophagic degradation.[11] Interestingly, independent of autophagosomes, a single soluble LC3 is associated with an approximately 500 kDa complex in the cytoplasm.[12]

Nuclear LC3

The importance of the nuclear functions of autophagy proteins should not be underestimated. A large pool of LC3 is present in the nucleus of a variety of different cell types.[13] In response to starvation, nuclear LC3 is deacetylated and trafficked out of the nucleus into the cytoplasm where it functions in autophagy.[14] Nuclear LC3 interacts with lamin B1, and participates in the degradation of nuclear lamina.[15] LC3 is also enriched in nucleoli via its triple arginine motif, and associates with a number of different nuclear and nucleolar constituents including: MAP1B, tubulin, and several ribosomal proteins.[16]

Structure

LC3 shares structural homology with ubiquitin, and thus has been termed a ubiquitin-like protein.[17] LC3 has a LDS (LIR docking site)/hydrophobic binding interface in the N terminus which interacts with LIR (LC3 Interacting Region) containing proteins.[12] This domain is rich in hydrophobic amino acids, the mutation of which impairs the ability of LC3 binding with LIR containing proteins, many of which are autophagy cargo adapter proteins. For example, sequestosome (SQSTM1) interacts with Phe 52 and Leu53 aminoacids present in hydrophobic binding interface of LC3 and any mutation of these amino acids prevents LC3 interaction with SQSTM1.

Post-translational regulation

References

  1. "Entrez Gene: MAP1LC3B microtubule-associated protein 1 light chain 3 beta".
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Further reading

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