View source for RAC1

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{{Infobox_gene}}
'''Rac1''', also known as '''Ras-related C3 botulinum toxin substrate 1''', is a [[protein]] found in human cells. It is encoded by the ''RAC1'' [[gene]].<ref name="pmid2674130">{{cite journal | vauthors = Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R | title = rac, a novel ras-related family of proteins that are botulinum toxin substrates | journal = The Journal of Biological Chemistry | volume = 264 | issue = 28 | pages = 16378–82 | date = Oct 1989 | pmid = 2674130 | doi =  }}</ref><ref name="pmid10597294">{{cite journal | vauthors = Jordan P, Brazåo R, Boavida MG, Gespach C, Chastre E | title = Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors | journal = Oncogene | volume = 18 | issue = 48 | pages = 6835–9 | date = Nov 1999 | pmid = 10597294 | doi = 10.1038/sj.onc.1203233 }}</ref> This gene can produce a variety of [[Alternative splicing|alternatively spliced]] versions of the Rac1 protein, which appear to carry out different functions.<ref name="pmid22430205">{{cite journal | vauthors = Zhou C, Licciulli S, Avila JL, Cho M, Troutman S, Jiang P, Kossenkov AV, Showe LC, Liu Q, Vachani A, Albelda SM, Kissil JL | title = The Rac1 splice form Rac1b promotes K-ras-induced lung tumorigenesis | journal = Oncogene | volume = 32 | issue = 7 | pages = 903–9 | date = Feb 2013 | pmid = 22430205 | pmc = 3384754 | doi = 10.1038/onc.2012.99 }}</ref>

== Function ==

Rac1 is a small (~21 kDa) signaling [[G protein]] (more specifically a [[GTPase]]), and is a member of the [[Rac protein|Rac]] subfamily of the family [[Rho family of GTPases]]. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of [[GLUT4]]<ref name=":0">{{Cite journal|last=Sylow|first=Lykke|last2=Nielsen|first2=Ida L.|last3=Kleinert|first3=Maximilian|last4=Møller|first4=Lisbeth L. V.|last5=Ploug|first5=Thorkil|last6=Schjerling|first6=Peter|last7=Bilan|first7=Philip J.|last8=Klip|first8=Amira|last9=Jensen|first9=Thomas E.|date=2016-04-09|title=Rac1 governs exercise-stimulated glucose uptake in skeletal muscle through regulation of GLUT4 translocation in mice|journal=The Journal of Physiology|volume=594|issue=17|pages=4997–5008|doi=10.1113/JP272039|issn=1469-7793|pmid=27061726|pmc=5009787}}</ref><ref name=":1" /> translocation to glucose uptake, [[cell growth]], [[cytoskeleton|cytoskeletal]] reorganization, antimicrobial cytotoxicity,<ref name="pmid26867574">{{cite journal | vauthors = Xiang RF | title = Ras-related C3 Botulinum Toxin Substrate (Rac) and Src Family Kinases (SFK) Are Proximal and Essential for Phosphatidylinositol 3-Kinase (PI3K) Activation in Natural Killer (NK) Cell-mediated Direct Cytotoxicity against Cryptococcus neoformans | journal = J Biol Chem | volume = 291 | issue = 13 | pages = 6912–22 | date = Mar 2016 | pmid = 26867574 | doi = 10.1074/jbc.M115.681544 | pmc=4807276}}</ref> and the activation of protein [[kinase]]s.<ref name="pmid16949823">{{cite journal | vauthors = Ridley AJ | title = Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking | journal = Trends in Cell Biology | volume = 16 | issue = 10 | pages = 522–9 | date = Oct 2006 | pmid = 16949823 | doi = 10.1016/j.tcb.2006.08.006 }}</ref>

Rac1 is a [[pleiotropic]] regulator of many cellular processes, including the cell cycle, cell-cell adhesion, [[motility]] (through the actin network), and of [[epithelial]] [[cellular differentiation|differentiation]] (proposed to be necessary for maintaining epidermal stem cells).

== Role in cancer ==

Along with other subfamily of Rac and Rho proteins, they exert an important regulatory role specifically in cell motility and cell growth. Rac1 has ubiquitous tissue expression, and drives cell motility by formation of [[lamellipodia]].<ref name="parri">{{cite journal | vauthors = Parri M, Chiarugi P | title = Rac and Rho GTPases in cancer cell motility control | journal = Cell Communication and Signaling | volume = 8 | issue = 23 | pages = 23 | date = 2010 | pmid =  20822528| pmc = 2941746 | doi = 10.1186/1478-811x-8-23 }}</ref> In order for cancer cells to grow and invade local and distant tissues, deregulation of cell motility is one of the hallmark events in cancer cell invasion and metastasis.<ref name="hallmarks">{{cite journal | vauthors = Hanahan D, Weinberg RA | title = Hallmarks of cancer: the next generation | journal = Cell | volume = 144 | issue = 5 | pages = 646–74 | date = Mar 2011 | pmid = 21376230 | doi = 10.1016/j.cell.2011.02.013 }}</ref> Overexpression of a constitutively active Rac1 V12 in mice caused a tumor that's phenotypically indistinguishable from human Kaposi's sarcoma.<ref>{{Cite journal|last=Ma|first=Qi|last2=Cavallin|first2=Lucas E.|last3=Yan|first3=Bin|last4=Zhu|first4=Shoukang|last5=Duran|first5=Elda Margarita|last6=Wang|first6=Huili|last7=Hale|first7=Laura P.|last8=Dong|first8=Chunming|last9=Cesarman|first9=Ethel|date=2009-05-26|title=Antitumorigenesis of antioxidants in a transgenic Rac1 model of Kaposi's sarcoma|url=http://www.pnas.org/content/106/21/8683|journal=Proceedings of the National Academy of Sciences|language=en|volume=106|issue=21|pages=8683–8688|doi=10.1073/pnas.0812688106|issn=0027-8424|pmc=2679580|pmid=19429708}}</ref> Activating or gain-of-function mutations of Rac1 are shown to play active roles in promoting mesenchymal-type of cell movement assisted by [[NEDD9]] and [[DOCK3]] protein complex.<ref name="sanz">{{cite journal | vauthors = Sanz-Moreno V, Gadea G, Ahn J, Paterson H, Marra P, Pinner S, Sahai E, Marshall CJ | title = Rac activation and inactivation control plasticity of tumor cell movement | journal = Cell | volume = 135 | issue = 3 | pages = 510–23 | date = Oct 2008 | pmid = 18984162 | doi = 10.1016/j.cell.2008.09.043 }}</ref> Such abnormal cell motility may result in [[epithelial mesenchymal transition]] (EMT) – a driving mechanism for tumor metastasis as well as drug-resistant tumor relapse.<ref name="stallmann">{{cite journal  |vauthors=Stallings-Mann ML, Waldmann J, Zhang Y, Miller E, Gauthier ML, Visscher DW, etal | title = Matrix metalloproteinase induction of Rac1b, a key effector of lung cancer progression | journal = Science Translational Medicine | volume = 4 | issue = 142 | pages = 510–523 |date=Jul 11, 2012 | pmid = | doi = | url =  }}</ref><ref name="yang">{{cite journal | vauthors = Yang WH, Lan HY, Huang CH, Tai SK, Tzeng CH, Kao SY, Wu KJ, Hung MC, Yang MH | title = RAC1 activation mediates Twist1-induced cancer cell migration | journal = Nature Cell Biology | volume = 14 | issue = 4 | pages = 366–74 | date = Apr 2012 | pmid =  22407364| doi = 10.1038/ncb2455 }}</ref>

== Role in glucose transport==

Rac1 is expressed in significant amounts in insulin sensitive tissues, such as adipose tissue and skeletal muscle. Here Rac1 regulated the translocation of glucose transporting [[GLUT4]] vesicles from intracellular compartments to the plasma membrane.<ref name=":1">{{cite journal | vauthors = Ueda S, Kitazawa S, Ishida K, Nishikawa Y, Matsui M, Matsumoto H, Aoki T, Nozaki S, Takeda T, Tamori Y, Aiba A, Kahn CR, Kataoka T, Satoh T | title = Crucial role of the small GTPase Rac1 in insulin-stimulated translocation of glucose transporter 4 to the mouse skeletal muscle sarcolemma | journal = FASEB Journal | volume = 24 | issue = 7 | pages = 2254–61 | date = Jul 2010 | pmc = 4183928 | doi = 10.1096/fj.09-137380 | pmid = 20203090}}</ref><ref>{{cite journal | vauthors = Sylow L, Kleinert M, Pehmøller C, Prats C, Chiu TT, Klip A, Richter EA, Jensen TE | title = Akt and Rac1 signaling are jointly required for insulin-stimulated glucose uptake in skeletal muscle and downregulated in insulin resistance | journal = Cellular Signalling | volume = 26 | issue = 2 | pages = 323–31 | date = Feb 2014 | doi = 10.1016/j.cellsig.2013.11.007 | pmid = 24216610 }}</ref><ref>{{cite journal | vauthors = Sylow L, Jensen TE, Kleinert M, Højlund K, Kiens B, Wojtaszewski J, Prats C, Schjerling P, Richter EA | title = Rac1 signaling is required for insulin-stimulated glucose uptake and is dysregulated in insulin-resistant murine and human skeletal muscle | journal = Diabetes | volume = 62 | issue = 6 | pages = 1865–75 | date = Jun 2013 | pmc = 3661612 | doi = 10.2337/db12-1148 | pmid = 23423567 }}</ref> In response to [[insulin]], this allows for blood glucose to enter the cell to lower blood glucose. In conditions of [[obesity]] and [[type 2 diabetes]], Rac1 signaling in skeletal muscle is dysfunctional, suggesting that Rac1 contributes to the progression of the disease. 
Rac1 protein is also necessary for glucose uptake in skeletal muscle activated by exercise<ref name=":0" /><ref>{{cite journal | vauthors = Sylow L, Jensen TE, Kleinert M, Mouatt JR, Maarbjerg SJ, Jeppesen J, Prats C, Chiu TT, Boguslavsky S, Klip A, Schjerling P, Richter EA | title = Rac1 is a novel regulator of contraction-stimulated glucose uptake in skeletal muscle | journal = Diabetes | volume = 62 | issue = 4 | pages = 1139–51 | date = Apr 2013 | pmc = 3609592 | doi = 10.2337/db12-0491 | pmid = 23274900 }}</ref>  and muscle stretching<ref>{{cite journal | vauthors = Sylow L, Møller LL, Kleinert M, Richter EA, Jensen TE | title = Stretch-stimulated glucose transport in skeletal muscle is regulated by Rac1 | journal = The Journal of Physiology | volume = 593 | issue = 3 | pages = 645–56 | date = Feb 2015 | pmc = 4324711 | doi = 10.1113/jphysiol.2014.284281 | pmid = 25416624 }}</ref>

== Clinical significance ==

Activating mutations in Rac1 have been recently discovered in large-scale genomic studies involving [[melanoma]] <ref name="pmid22817889">{{cite journal | vauthors = Hodis E, Watson IR, Kryukov GV, Arold ST, Imielinski M, Theurillat JP, Nickerson E, Auclair D, Li L, Place C, Dicara D, Ramos AH, Lawrence MS, Cibulskis K, Sivachenko A, Voet D, Saksena G, Stransky N, Onofrio RC, Winckler W, Ardlie K, Wagle N, Wargo J, Chong K, Morton DL, Stemke-Hale K, Chen G, Noble M, Meyerson M, Ladbury JE, Davies MA, Gershenwald JE, Wagner SN, Hoon DS, Schadendorf D, Lander ES, Gabriel SB, Getz G, Garraway LA, Chin L | title = A landscape of driver mutations in melanoma | journal = Cell | volume = 150 | issue = 2 | pages = 251–63 | date = Jul 2012 | pmid = 22817889 | pmc = 3600117 | doi = 10.1016/j.cell.2012.06.024 }}</ref><ref name="pmid22842228">{{cite journal | vauthors = Krauthammer M, Kong Y, Ha BH, Evans P, Bacchiocchi A, McCusker JP, Cheng E, Davis MJ, Goh G, Choi M, Ariyan S, Narayan D, Dutton-Regester K, Capatana A, Holman EC, Bosenberg M, Sznol M, Kluger HM, Brash DE, Stern DF, Materin MA, Lo RS, Mane S, Ma S, Kidd KK, Hayward NK, Lifton RP, Schlessinger J, Boggon TJ, Halaban R | title = Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma | journal = Nature Genetics | volume = 44 | issue = 9 | pages = 1006–14 | date = Sep 2012 | pmid = 22842228 | pmc = 3432702 | doi = 10.1038/ng.2359 }}</ref><ref name="pmid17904119">{{cite journal | vauthors = Bauer NN, Chen YW, Samant RS, Shevde LA, Fodstad O | title = Rac1 activity regulates proliferation of aggressive metastatic melanoma | journal = Experimental Cell Research | volume = 313 | issue = 18 | pages = 3832–9 | date = Nov 2007 | pmid = 17904119 | doi = 10.1016/j.yexcr.2007.08.017 }}</ref> and [[non-small cell lung cancer]].<ref name="pmid22786680">{{cite journal | vauthors = Stallings-Mann ML, Waldmann J, Zhang Y, Miller E, Gauthier ML, Visscher DW, Downey GP, Radisky ES, Fields AP, Radisky DC | title = Matrix metalloproteinase induction of Rac1b, a key effector of lung cancer progression | journal = Science Translational Medicine | volume = 4 | issue = 142 | pages = 142ra95 | date = Jul 2012 | pmid = 22786680 | pmc = 3733503 | doi = 10.1126/scitranslmed.3004062 }}</ref> As a result, Rac1 is considered a therapeutic target for many of these diseases.<ref name="pmid22786678">{{cite journal | vauthors = McAllister SS | title = Got a light? Illuminating lung cancer | journal = Science Translational Medicine | volume = 4 | issue = 142 | pages = 142fs22 | date = Jul 2012 | pmid = 22786678 | doi = 10.1126/scitranslmed.3004446 }}</ref>

A few recent studies have also exploited targeted therapy to suppress tumor growth by pharmacological inhibition of Rac1 activity in metastatic melanoma and liver cancer as well as in human breast cancer.<ref name="chen">{{cite journal  |vauthors=Chen QY, Xu LQ, Jiao DM, Yao QH, Wang YY, Hu HZ, etal | title = Silencing of Rac1 modifies lung cancer cell migration, invasion and actin cytoskeleton rearrangements and enhances chemosensitivity to antitumor drugs | journal = International Journal of Molecular Medicine| volume = 28 | issue = 5 | pages = 769–776 |date=Nov 2011 | pmid = | doi = | url =  }}</ref><ref name="dok">{{cite journal | vauthors = Dokmanovic M, Hirsch DS, Shen Y, Wu WJ | title = Rac1 contributes to trastuzumab resistance of breast cancer cells: Rac1 as a potential therapeutic target for the treatment of trastuzumab-resistant breast cancer | journal = Molecular Cancer Therapeutics | volume = 8 | issue = 6 | pages = 1557–69 | date = Jun 2009 | pmid =  19509242| doi = 10.1158/1535-7163.mct-09-0140 }}</ref><ref name="liu">{{cite journal | vauthors = Liu S, Yu M, He Y, Xiao L, Wang F, Song C, Sun S, Ling C, Xu Z | title = Melittin prevents liver cancer cell metastasis through inhibition of the Rac1-dependent pathway | journal = Hepatology | volume = 47 | issue = 6 | pages = 1964–73 | date = Jun 2008 | pmid =  18506888| doi = 10.1002/hep.22240 }}</ref>
For example, Rac1-dependent pathway inhibition resulted in the reversal of tumor cell phenotypes, suggesting Rac1 as a predictive marker and therapeutic target for trastuzumab-resistant breast cancer.<ref name="dok"/> However, given Rac1's role in glucose transport, drugs that inhibits Rac1 could potentially be harmful to glucose homeostasis.

[[Dominant negative]] or [[Gene expression|constitutively active]] [[germline]] RAC1 mutations cause diverse [[phenotypes]] that have been grouped together as [https://omim.org/entry/617751 Mental Retardation Type 48].<ref>{{cite journal|last1=Reijnders|first1=Margot R.F.|last2=Ansor|first2=Nurhuda M.|last3=Kousi|first3=Maria|last4=Yue|first4=Wyatt W.|last5=Tan|first5=Perciliz L.|last6=Clarkson|first6=Katie|last7=Clayton-Smith|first7=Jill|last8=Corning|first8=Ken|last9=Jones|first9=Julie R.|last10=Lam|first10=Wayne W.K.|last11=Mancini|first11=Grazia M.S.|last12=Marcelis|first12=Carlo|last13=Mohammed|first13=Shehla|last14=Pfundt|first14=Rolph|last15=Roifman|first15=Maian|last16=Cohn|first16=Ronald|last17=Chitayat|first17=David|last18=Millard|first18=Tom H.|last19=Katsanis|first19=Nicholas|last20=Brunner|first20=Han G.|last21=Banka|first21=Siddharth|title=RAC1  Missense Mutations in Developmental Disorders with Diverse Phenotypes|journal=The American Journal of Human Genetics|date=September 2017|volume=101|issue=3|pages=466–477|doi=10.1016/j.ajhg.2017.08.007|pmid=28886345|pmc=5591022}}</ref> Most [[mutations]] cause [[microcephaly]] while some specific changes appear to result in [[macrocephaly]].

== Interactions ==

RAC1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ARFIP2]],<ref name = pmid11478794>{{cite journal | vauthors = Shin OH, Exton JH | title = Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1 | journal = Biochemical and Biophysical Research Communications | volume = 285 | issue = 5 | pages = 1267–73 | date = Aug 2001 | pmid = 11478794 | doi = 10.1006/bbrc.2001.5330 }}</ref><ref name = pmid8670882>{{cite journal | vauthors = Van Aelst L, Joneson T, Bar-Sagi D | title = Identification of a novel Rac1-interacting protein involved in membrane ruffling | journal = The EMBO Journal | volume = 15 | issue = 15 | pages = 3778–86 | date = Aug 1996 | pmid = 8670882 | pmc = 452058 | doi =  }}</ref><ref name = pmid11346801>{{cite journal | vauthors = Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ | title = The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways | journal = Nature | volume = 411 | issue = 6834 | pages = 215–9 | date = May 2001 | pmid = 11346801 | doi = 10.1038/35075620 }}</ref>
* [[ARHGDIA]],<ref name = pmid17353931>{{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}</ref><ref name = pmid11513578>{{cite journal | vauthors = Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E | title = Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation | journal = Biochemistry | volume = 40 | issue = 34 | pages = 10007–13 | date = Aug 2001 | pmid = 11513578 | doi = 10.1021/bi010288k }}</ref><ref name = pmid10673424>{{cite journal | vauthors = Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC | title = Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1 | journal = Structure | volume = 8 | issue = 1 | pages = 47–55 | date = Jan 2000 | pmid = 10673424 | doi = 10.1016/S0969-2126(00)00080-0 }}</ref><ref name = pmid9490022>{{cite journal | vauthors = Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P | title = Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity | journal = FEBS Letters | volume = 422 | issue = 2 | pages = 269–73 | date = Jan 1998 | pmid = 9490022 | doi = 10.1016/S0014-5793(98)00020-9 }}</ref><ref name = pmid11513579>{{cite journal | vauthors = Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC | title = Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex | journal = Biochemistry | volume = 40 | issue = 34 | pages = 10014–22 | date = Aug 2001 | pmid = 11513579 | doi = 10.1021/bi010289c }}</ref><ref name = pmid11368848>{{cite journal | vauthors = Fauré J, Dagher MC | title = Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI) | journal = Biochimie | volume = 83 | issue = 5 | pages = 409–14 | date = May 2001 | pmid = 11368848 | doi = 10.1016/S0300-9084(01)01263-9 }}</ref>
* [[BAIAP2]],<ref name = pmid11130076>{{cite journal | vauthors = Miki H, Yamaguchi H, Suetsugu S, Takenawa T | title = IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling | journal = Nature | volume = 408 | issue = 6813 | pages = 732–5 | date = Dec 2000 | pmid = 11130076 | doi = 10.1038/35047107 }}</ref>
* [[FHOD1]],<ref name = pmid11590143>{{cite journal | vauthors = Westendorf JJ | title = The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element | journal = The Journal of Biological Chemistry | volume = 276 | issue = 49 | pages = 46453–9 | date = Dec 2001 | pmid = 11590143 | doi = 10.1074/jbc.M105162200 }}</ref>
* [[FMNL1]],<ref name = pmid10958683>{{cite journal | vauthors = Yayoshi-Yamamoto S, Taniuchi I, Watanabe T | title = FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages | journal = Molecular and Cellular Biology | volume = 20 | issue = 18 | pages = 6872–81 | date = Sep 2000 | pmid = 10958683 | pmc = 86228 | doi = 10.1128/MCB.20.18.6872-6881.2000 }}</ref>
* [[IQGAP1]],<ref name = pmid9535855/><ref name = pmid8798539>{{cite journal | vauthors = Kuroda S, Fukata M, Kobayashi K, Nakafuku M, Nomura N, Iwamatsu A, Kaibuchi K | title = Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 38 | pages = 23363–7 | date = Sep 1996 | pmid = 8798539 | doi = 10.1074/jbc.271.38.23363 }}</ref><ref name = pmid12110184>{{cite journal | vauthors = Fukata M, Watanabe T, Noritake J, Nakagawa M, Yamaga M, Kuroda S, Matsuura Y, Iwamatsu A, Perez F, Kaibuchi K | title = Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170 | journal = Cell | volume = 109 | issue = 7 | pages = 873–85 | date = Jun 2002 | pmid = 12110184 | doi = 10.1016/S0092-8674(02)00800-0 }}</ref><ref name = pmid8670801>{{cite journal | vauthors = Hart MJ, Callow MG, Souza B, Polakis P | title = IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs | journal = The EMBO Journal | volume = 15 | issue = 12 | pages = 2997–3005 | date = Jun 1996 | pmid = 8670801 | pmc = 450241 | doi =  }}</ref>
* [[IQGAP2]],<ref name = pmid8756646>{{cite journal | vauthors = Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ | title = The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases | journal = Molecular and Cellular Biology | volume = 16 | issue = 9 | pages = 4869–78 | date = Sep 1996 | pmid = 8756646 | pmc = 231489 | doi =  10.1128/mcb.16.9.4869}}</ref>
* [[Myd88]],<ref name = pmid11416133>{{cite journal | vauthors = Jefferies C, Bowie A, Brady G, Cooke EL, Li X, O'Neill LA | title = Transactivation by the p65 subunit of NF-kappaB in response to interleukin-1 (IL-1) involves MyD88, IL-1 receptor-associated kinase 1, TRAF-6, and Rac1 | journal = Molecular and Cellular Biology | volume = 21 | issue = 14 | pages = 4544–52 | date = Jul 2001 | pmid = 11416133 | pmc = 87113 | doi = 10.1128/MCB.21.14.4544-4552.2001 | url = http://www.tara.tcd.ie/bitstream/2262/33698/1/Transactivation%20by%20the%20p65%20subunit%20of%20NF-kappaB%20in%20response%20to%20interleukin-1%20%28IL-1%29%20involves%20MyD88%2c%20IL-1%20receptor-associated%20kinase%201%2c%20TRAF-6%2c%20and%20Rac1.pdf }}</ref>
* [[Myotonic dystrophy protein kinase|DMPK]],<ref name = pmid10869570>{{cite journal | vauthors = Shimizu M, Wang W, Walch ET, Dunne PW, Epstein HF | title = Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase | journal = FEBS Letters | volume = 475 | issue = 3 | pages = 273–7 | date = Jun 2000 | pmid = 10869570 | doi = 10.1016/S0014-5793(00)01692-6 }}</ref>
* [[NCKAP1]],<ref name = pmid9148763>{{cite journal | vauthors = Kitamura Y, Kitamura T, Sakaue H, Maeda T, Ueno H, Nishio S, Ohno S, Osada S, Sakaue M, Ogawa W, Kasuga M | title = Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac | journal = The Biochemical Journal | volume = 322 | issue = 3 | pages = 873–8 | date = Mar 1997 | pmid = 9148763 | pmc = 1218269 | doi =  10.1042/bj3220873}}</ref>
* [[PAK1]],<ref name = pmid9535855>{{cite journal | vauthors = Zhang B, Chernoff J, Zheng Y | title = Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA | journal = The Journal of Biological Chemistry | volume = 273 | issue = 15 | pages = 8776–82 | date = Apr 1998 | pmid = 9535855 | doi = 10.1074/jbc.273.15.8776 }}</ref><ref name = pmid12879077>{{cite journal | vauthors = Katoh H, Negishi M | title = RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo | journal = Nature | volume = 424 | issue = 6947 | pages = 461–4 | date = Jul 2003 | pmid = 12879077 | doi = 10.1038/nature01817 }}</ref><ref name = pmid12650940>{{cite journal | vauthors = Seoh ML, Ng CH, Yong J, Lim L, Leung T | title = ArhGAP15, a novel human RacGAP protein with GTPase binding property | journal = FEBS Letters | volume = 539 | issue = 1–3 | pages = 131–7 | date = Mar 2003 | pmid = 12650940 | doi = 10.1016/S0014-5793(03)00213-8 }}</ref>
* [[PAK3]],<ref name = pmid11478794/>
* [[PARD6A]],<ref name = pmid11260256/><ref name = pmid10873802>{{cite journal | vauthors = Qiu RG, Abo A, Steven Martin G | title = A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCzeta signaling and cell transformation | journal = Current Biology | volume = 10 | issue = 12 | pages = 697–707 | date = Jun 2000 | pmid = 10873802 | doi = 10.1016/S0960-9822(00)00535-2 }}</ref>
* [[PARD6B]],<ref name = pmid11260256>{{cite journal | vauthors = Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H | title = Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C | journal = Genes to Cells | volume = 6 | issue = 2 | pages = 107–19 | date = Feb 2001 | pmid = 11260256 | doi = 10.1046/j.1365-2443.2001.00404.x }}</ref>
* [[RICS (gene)|RICS]]<ref name = pmid12819203>{{cite journal | vauthors = Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS | title = GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 36 | pages = 34641–53 | date = Sep 2003 | pmid = 12819203 | doi = 10.1074/jbc.M304594200 }}</ref><ref name = pmid12454018>{{cite journal | vauthors = Moon SY, Zang H, Zheng Y | title = Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP | journal = The Journal of Biological Chemistry | volume = 278 | issue = 6 | pages = 4151–9 | date = Feb 2003 | pmid = 12454018 | doi = 10.1074/jbc.M207789200 }}</ref>
* [[STAT3]],<ref name = pmid11021801>{{cite journal | vauthors = Simon AR, Vikis HG, Stewart S, Fanburg BL, Cochran BH, Guan KL | title = Regulation of STAT3 by direct binding to the Rac1 GTPase | journal = Science | volume = 290 | issue = 5489 | pages = 144–7 | date = Oct 2000 | pmid = 11021801 | doi = 10.1126/science.290.5489.144 }}</ref>  and
* [[T-cell lymphoma invasion and metastasis-inducing protein 1|TIAM1]].<ref name = pmid11130063>{{cite journal | vauthors = Worthylake DK, Rossman KL, Sondek J | title = Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1 | journal = Nature | volume = 408 | issue = 6813 | pages = 682–8 | date = Dec 2000 | pmid = 11130063 | doi = 10.1038/35047014 }}</ref><ref name = pmid11595749>{{cite journal | vauthors = Gao Y, Xing J, Streuli M, Leto TL, Zheng Y | title = Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors | journal = The Journal of Biological Chemistry | volume = 276 | issue = 50 | pages = 47530–41 | date = Dec 2001 | pmid = 11595749 | doi = 10.1074/jbc.M108865200 }}</ref>
{{Div col end}}
{{Clear}}

== References ==
{{Reflist|33em}}

== Further reading ==
{{Refbegin|33em}}
* {{cite journal | vauthors = Benitah SA, Frye M, Glogauer M, Watt FM | title = Stem cell depletion through epidermal deletion of Rac1 | journal = Science | volume = 309 | issue = 5736 | pages = 933–5 | date = Aug 2005 | pmid = 16081735 | doi = 10.1126/science.1113579 }}
* {{cite journal | vauthors = Ramakers GJ | title = Rho proteins, mental retardation and the cellular basis of cognition | journal = Trends in Neurosciences | volume = 25 | issue = 4 | pages = 191–9 | date = Apr 2002 | pmid = 11998687 | doi = 10.1016/S0166-2236(00)02118-4 }}
* {{cite journal | vauthors = Esufali S, Charames GS, Bapat B | title = Suppression of nuclear Wnt signaling leads to stabilization of Rac1 isoforms | journal = FEBS Letters | volume = 581 | issue = 25 | pages = 4850–6 | date = Oct 2007 | pmid = 17888911 | doi = 10.1016/j.febslet.2007.09.013 }}
{{Refend}}

== External links ==
* {{MeshName|rac1+GTP-Binding+Protein}}
*[https://web.archive.org/web/20110722013437/http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=5879 RAC1] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]

{{PDB Gallery|geneid=5879}}
{{GTPases}}
{{Rho family of GTPases}}