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{{ | '''Endophilin-A1''' is a [[protein]] that in humans is encoded by the ''SH3GL2'' [[gene]].<ref name="pmid9169142">{{cite journal |author1=Giachino C |author2=Lantelme E |author3=Lanzetti L |author4=Saccone S |author5=Bella Valle G |author6=Migone N | title = A novel SH3-containing human gene family preferentially expressed in the central nervous system | journal = Genomics | volume = 41 | issue = 3 | pages = 427–34 |date=Jul 1997 | pmid = 9169142 | pmc = | doi =10.1006/geno.1997.4645 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SH3GL2 SH3-domain GRB2-like 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6456| accessdate = }}</ref> | ||
}} | |||
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==Interactions== | |||
SH3GL2 has been shown to [[Protein-protein interaction|interact]] with [[DNM1]],<ref name=pmid9341169>{{cite journal |doi=10.1074/jbc.272.43.27239 |last=Micheva |first=K D |authorlink= |author2=Kay B K |author3=McPherson P S |date=Oct 1997 |title=Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin |journal=J. Biol. Chem. |volume=272 |issue=43 |pages=27239–45 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9341169 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid12456676>{{cite journal |last=Modregger |first=Jan |authorlink= |author2=Schmidt Anne A |author3=Ritter Brigitte |author4=Huttner Wieland B |author5=Plomann Markus |date=Feb 2003 |title=Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1 |journal=J. Biol. Chem. |volume=278 |issue=6 |pages=4160–7 |publisher= |location = United States| issn = 0021-9258| pmid = 12456676 |doi = 10.1074/jbc.M208568200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Amphiphysin]],<ref name=pmid9341169/><ref name=pmid12456676/> [[ADAM9]],<ref name=pmid10531379>{{cite journal |doi=10.1074/jbc.274.44.31693 |last=Howard |first=L |authorlink= |author2=Nelson K K |author3=Maciewicz R A |author4=Blobel C P |date=Oct 1999 |title=Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1 |journal=J. Biol. Chem. |volume=274 |issue=44 |pages=31693–9 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10531379 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[SH3KBP1]]<ref name=pmid11894095>{{cite journal |last=Soubeyran |first=Philippe |authorlink= |author2=Kowanetz Katarzyna |author3=Szymkiewicz Iwona |author4=Langdon Wallace Y |author5=Dikic Ivan |date=Mar 2002 |title=Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors |journal=[[Nature (journal)|Nature]] |volume=416 |issue=6877 |pages=183–7 |publisher= |location = England| issn = 0028-0836| pmid = 11894095 |doi = 10.1038/416183a | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[ADAM15]].<ref name=pmid10531379/> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
*{{cite journal | author=Ren Y, Fang F, Davey F, Taylor M, Aiton J, Coote P, Yao J, Chen JX, Yan SD & Gunn-Moore FJ. |title=Endophilin I expression is increased in the brains of Alzheimer’s disease patients. |journal=Journal of Biological Chemistry |volume=283 |pages= 5685–91 |year= 2008 | pmid=18167351 | issue=9 | doi=10.1074/jbc.M707932200}} | |||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |author1=Reutens AT |author2=Begley CG |title=Endophilin-1: a multifunctional protein. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 10 |pages= 1173–7 |year= 2002 |pmid= 12127567 |doi=10.1016/S1357-2725(02)00063-8 }} | ||
*{{cite journal | *{{cite journal |vauthors=So CW, Caldas C, Liu MM, etal |title=EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 6 |pages= 2563–8 |year= 1997 |pmid= 9122235 |doi=10.1073/pnas.94.6.2563 | pmc=20128 }} | ||
*{{cite journal |author1=Ringstad N |author2=Nemoto Y |author3=De Camilli P |title=The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8569–74 |year= 1997 |pmid= 9238017 |doi=10.1073/pnas.94.16.8569 | pmc=23017 }} | |||
*{{cite journal |author1=Micheva KD |author2=Ramjaun AR |author3=Kay BK |author4=McPherson PS |title=SH3 domain-dependent interactions of endophilin with amphiphysin. |journal=FEBS Lett. |volume=414 |issue= 2 |pages= 308–12 |year= 1997 |pmid= 9315708 |doi=10.1016/S0014-5793(97)01016-8 }} | |||
*{{cite journal |author1=Micheva KD |author2=Kay BK |author3=McPherson PS |title=Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27239–45 |year= 1997 |pmid= 9341169 |doi=10.1074/jbc.272.43.27239 }} | |||
*{{cite journal | | *{{cite journal |author1=Howard L |author2=Nelson KK |author3=Maciewicz RA |author4=Blobel CP |title=Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31693–9 |year= 1999 |pmid= 10531379 |doi=10.1074/jbc.274.44.31693 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Tang Y, Hu LA, Miller WE, etal |title=Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 22 |pages= 12559–64 |year= 1999 |pmid= 10535961 |doi=10.1073/pnas.96.22.12559 | pmc=22990 }} | ||
*{{cite journal | *{{cite journal |vauthors=Cestra G, Castagnoli L, Dente L, etal |title=The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity. |journal=J. Biol. Chem. |volume=274 |issue= 45 |pages= 32001–7 |year= 1999 |pmid= 10542231 |doi=10.1074/jbc.274.45.32001 }} | ||
*{{cite journal | *{{cite journal |vauthors=So CW, So CK, Cheung N, etal |title=The interaction between EEN and Abi-1, two MLL fusion partners, and synaptojanin and dynamin: implications for leukaemogenesis. |journal=Leukemia |volume=14 |issue= 4 |pages= 594–601 |year= 2000 |pmid= 10764144 |doi=10.1038/sj.leu.2401692 }} | ||
*{{cite journal | *{{cite journal |vauthors=So CW, Sham MH, Chew SL, etal |title=Expression and protein-binding studies of the EEN gene family, new interacting partners for dynamin, synaptojanin and huntingtin proteins. | volume=348 |journal=Biochem. J. |issue= 2|pages= 447–58 |year= 2000 |pmid= 10816441 |doi=10.1042/0264-6021:3480447 | pmc=1221085 }} | ||
*{{cite journal | *{{cite journal |vauthors=Zucconi A, Dente L, Santonico E, etal |title=Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. |journal=J. Mol. Biol. |volume=307 |issue= 5 |pages= 1329–39 |year= 2001 |pmid= 11292345 |doi= 10.1006/jmbi.2001.4572 }} | ||
*{{cite journal | *{{cite journal |vauthors=Ramjaun AR, Angers A, Legendre-Guillemin V, etal |title=Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 28913–9 |year= 2001 |pmid= 11384986 |doi= 10.1074/jbc.M103198200 }} | ||
*{{cite journal | *{{cite journal |author1=Chen-Hwang MC |author2=Chen HR |author3=Elzinga M |author4=Hwang YW |title=Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17597–604 |year= 2002 |pmid= 11877424 |doi= 10.1074/jbc.M111101200 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Soubeyran P, Kowanetz K, Szymkiewicz I, etal |title=Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. |journal=Nature |volume=416 |issue= 6877 |pages= 183–7 |year= 2002 |pmid= 11894095 |doi= 10.1038/416183a }} | ||
*{{cite journal | *{{cite journal |vauthors=Petrelli A, Gilestro GF, Lanzardo S, etal |title=The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met. |journal=Nature |volume=416 |issue= 6877 |pages= 187–90 |year= 2002 |pmid= 11894096 |doi= 10.1038/416187a }} | ||
*{{cite journal | *{{cite journal |vauthors=Chatellard-Causse C, Blot B, Cristina N, etal |title=Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29108–15 |year= 2002 |pmid= 12034747 |doi= 10.1074/jbc.M204019200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Szymkiewicz I, Kowanetz K, Soubeyran P, etal |title=CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39666–72 |year= 2002 |pmid= 12177062 |doi= 10.1074/jbc.M205535200 }} | ||
*{{cite journal | *{{cite journal |author1=Haglund K |author2=Shimokawa N |author3=Szymkiewicz I |author4=Dikic I |title=Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 19 |pages= 12191–6 |year= 2002 |pmid= 12218189 |doi= 10.1073/pnas.192462299 | pmc=129420 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Verstreken P, Kjaerulff O, Lloyd TE, etal |title= Endophilin mutations block clathrin-mediated endocytosis but not neurotransmitter release. | ||
|journal= Cell |volume=109 |issue= 1 |pages= 101–12 |year= 2002 | |||
|pmid= 11955450 |doi= 10.1016/S0092-8674(02)00688-8 }} | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=6456}} | |||
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Revision as of 06:17, 11 September 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
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Endophilin-A1 is a protein that in humans is encoded by the SH3GL2 gene.[1][2]
Interactions
SH3GL2 has been shown to interact with DNM1,[3][4] Amphiphysin,[3][4] ADAM9,[5] SH3KBP1[6] and ADAM15.[5]
References
- ↑ Giachino C; Lantelme E; Lanzetti L; Saccone S; Bella Valle G; Migone N (Jul 1997). "A novel SH3-containing human gene family preferentially expressed in the central nervous system". Genomics. 41 (3): 427–34. doi:10.1006/geno.1997.4645. PMID 9169142.
- ↑ "Entrez Gene: SH3GL2 SH3-domain GRB2-like 2".
- ↑ 3.0 3.1 Micheva, K D; Kay B K; McPherson P S (Oct 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. UNITED STATES. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. ISSN 0021-9258. PMID 9341169.
- ↑ 4.0 4.1 Modregger, Jan; Schmidt Anne A; Ritter Brigitte; Huttner Wieland B; Plomann Markus (Feb 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. United States. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. ISSN 0021-9258. PMID 12456676.
- ↑ 5.0 5.1 Howard, L; Nelson K K; Maciewicz R A; Blobel C P (Oct 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. UNITED STATES. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. ISSN 0021-9258. PMID 10531379.
- ↑ Soubeyran, Philippe; Kowanetz Katarzyna; Szymkiewicz Iwona; Langdon Wallace Y; Dikic Ivan (Mar 2002). "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors". Nature. England. 416 (6877): 183–7. doi:10.1038/416183a. ISSN 0028-0836. PMID 11894095.
Further reading
- Ren Y, Fang F, Davey F, Taylor M, Aiton J, Coote P, Yao J, Chen JX, Yan SD & Gunn-Moore FJ. (2008). "Endophilin I expression is increased in the brains of Alzheimer's disease patients". Journal of Biological Chemistry. 283 (9): 5685–91. doi:10.1074/jbc.M707932200. PMID 18167351.
- Reutens AT; Begley CG (2002). "Endophilin-1: a multifunctional protein". Int. J. Biochem. Cell Biol. 34 (10): 1173–7. doi:10.1016/S1357-2725(02)00063-8. PMID 12127567.
- So CW, Caldas C, Liu MM, et al. (1997). "EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on chromosome 19p13 that fuses to MLL in human leukemia". Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2563–8. doi:10.1073/pnas.94.6.2563. PMC 20128. PMID 9122235.
- Ringstad N; Nemoto Y; De Camilli P (1997). "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8569–74. doi:10.1073/pnas.94.16.8569. PMC 23017. PMID 9238017.
- Micheva KD; Ramjaun AR; Kay BK; McPherson PS (1997). "SH3 domain-dependent interactions of endophilin with amphiphysin". FEBS Lett. 414 (2): 308–12. doi:10.1016/S0014-5793(97)01016-8. PMID 9315708.
- Micheva KD; Kay BK; McPherson PS (1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. PMID 9341169.
- Howard L; Nelson KK; Maciewicz RA; Blobel CP (1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379.
- Tang Y, Hu LA, Miller WE, et al. (1999). "Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12559–64. doi:10.1073/pnas.96.22.12559. PMC 22990. PMID 10535961.
- Cestra G, Castagnoli L, Dente L, et al. (1999). "The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity". J. Biol. Chem. 274 (45): 32001–7. doi:10.1074/jbc.274.45.32001. PMID 10542231.
- So CW, So CK, Cheung N, et al. (2000). "The interaction between EEN and Abi-1, two MLL fusion partners, and synaptojanin and dynamin: implications for leukaemogenesis". Leukemia. 14 (4): 594–601. doi:10.1038/sj.leu.2401692. PMID 10764144.
- So CW, Sham MH, Chew SL, et al. (2000). "Expression and protein-binding studies of the EEN gene family, new interacting partners for dynamin, synaptojanin and huntingtin proteins". Biochem. J. 348 (2): 447–58. doi:10.1042/0264-6021:3480447. PMC 1221085. PMID 10816441.
- Zucconi A, Dente L, Santonico E, et al. (2001). "Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1". J. Mol. Biol. 307 (5): 1329–39. doi:10.1006/jmbi.2001.4572. PMID 11292345.
- Ramjaun AR, Angers A, Legendre-Guillemin V, et al. (2001). "Endophilin regulates JNK activation through its interaction with the germinal center kinase-like kinase". J. Biol. Chem. 276 (31): 28913–9. doi:10.1074/jbc.M103198200. PMID 11384986.
- Chen-Hwang MC; Chen HR; Elzinga M; Hwang YW (2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424.
- Soubeyran P, Kowanetz K, Szymkiewicz I, et al. (2002). "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors". Nature. 416 (6877): 183–7. doi:10.1038/416183a. PMID 11894095.
- Petrelli A, Gilestro GF, Lanzardo S, et al. (2002). "The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met". Nature. 416 (6877): 187–90. doi:10.1038/416187a. PMID 11894096.
- Chatellard-Causse C, Blot B, Cristina N, et al. (2002). "Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization". J. Biol. Chem. 277 (32): 29108–15. doi:10.1074/jbc.M204019200. PMID 12034747.
- Szymkiewicz I, Kowanetz K, Soubeyran P, et al. (2002). "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases". J. Biol. Chem. 277 (42): 39666–72. doi:10.1074/jbc.M205535200. PMID 12177062.
- Haglund K; Shimokawa N; Szymkiewicz I; Dikic I (2002). "Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors". Proc. Natl. Acad. Sci. U.S.A. 99 (19): 12191–6. doi:10.1073/pnas.192462299. PMC 129420. PMID 12218189.
- Verstreken P, Kjaerulff O, Lloyd TE, et al. (2002). "Endophilin mutations block clathrin-mediated endocytosis but not neurotransmitter release". Cell. 109 (1): 101–12. doi:10.1016/S0092-8674(02)00688-8. PMID 11955450.
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