GIT1 (original) (raw)

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Protein-coding gene in humans

GIT1
Identifiers
Aliases	GIT1, GIT ArfGAP 1, p95-APP1
External IDs	OMIM: 608434; MGI: 1927140; HomoloGene: 32204; GeneCards: GIT1; OMA:GIT1 - orthologs
Gene location (Human)Chr.Chromosome 17 (human)[1]Band17q11.2Start29,573,475 bp[1]End29,594,054 bp[1]
Gene location (Mouse)Chr.Chromosome 11 (mouse)[2]Band11|11 B5Start77,384,388 bp[2]End77,398,612 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inright frontal lobecingulate gyrusanterior cingulate cortexolfactory bulbleft testisamygdalaprefrontal cortexcerebellar vermisputamenright testisTop expressed insuperior frontal gyrusprimary visual cortexperirhinal cortexentorhinal cortexdentate gyrus of hippocampal formation granule cellCA3 fieldankle jointseminiferous tubulespermatidhippocampus properMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular function protein-containing complex binding protein binding metal ion binding GTPase activator activity Cellular component membrane focal adhesion cytoplasm cytosol calyx of Held Biological process ephrin receptor signaling pathway positive regulation of GTPase activity regulation of cytokinesis regulation of G protein-coupled receptor signaling pathway presynaptic modulation of chemical synaptic transmission regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez28964216963EnsemblENSG00000108262ENSMUSG00000011877UniProtQ9Y2X7Q68FF6RefSeq (mRNA)NM_001085454NM_014030NM_001004144NM_001374758RefSeq (protein)NP_001078923NP_054749NP_001004144NP_001361687Location (UCSC)Chr 17: 29.57 – 29.59 MbChr 11: 77.38 – 77.4 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ARF GTPase-activating protein GIT1 is an enzyme that in humans is encoded by the GIT1 gene.[5][6][7]

GIT1 contains an ARFGAP domain, Anykrin repeats, and a GRK-interacting domain. The Arf-GAP domain, which enables it to act as a GTPase activating protein (GAP) for the Arf family of GTPases, has been shown to be involved in phosphorylation and inhibition of the ADRB2. If synaptic localization of GIT1 is disturbed, then this is known to affect dendritic spine morphology and formation—this is thought to occur through the Rac1/PAK1/LIMK/CFL1 pathway.[8]

GIT1 has been shown to interact with:

• ARHGEF7,[9][10]
• Beta adrenergic receptor kinase,[5][6]
• GIT2,[9]
• PCLO,[9]
• PLCG1,[11]
• PPFIA4[12][13]
• PTK2,[9][12][14] and
• liprin-alpha-1.[12][13]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108262 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000011877 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ a b Premont RT, Claing A, Vitale N, Freeman JL, Pitcher JA, Patton WA, Moss J, Vaughan M, Lefkowitz RJ (December 1998). "beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein". Proc Natl Acad Sci U S A. 95 (24): 14082–14087. Bibcode:1998PNAS...9514082P. doi:10.1073/pnas.95.24.14082. PMC 24330. PMID 9826657.
6. ^ a b Premont RT, Claing A, Vitale N, Perry SJ, Lefkowitz RJ (August 2000). "The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing". J Biol Chem. 275 (29): 22373–22380. doi:10.1074/jbc.275.29.22373. PMID 10896954.
7. ^ "Entrez Gene: GIT1 G protein-coupled receptor kinase interactor 1".
8. ^ Zhang H, Webb DJ, Asmussen H, Horwitz AF (2003). "Synapse formation is regulated by the signaling adaptor GIT1". J. Cell Biol. 161 (1): 131–142. doi:10.1083/jcb.200211002. PMC 2172873. PMID 12695502.
9. ^ a b c d Kim S, Ko J, Shin H, Lee JR, Lim C, Han JH, Altrock WD, Garner CC, Gundelfinger ED, Premont RT, Kaang BK, Kim E (February 2003). "The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo". J. Biol. Chem. 278 (8): 6291–300. doi:10.1074/jbc.M212287200. PMID 12473661.
10. ^ Bagrodia S, Bailey D, Lenard Z, Hart M, Guan JL, Premont RT, Taylor SJ, Cerione RA (August 1999). "A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins". J. Biol. Chem. 274 (32): 22393–400. doi:10.1074/jbc.274.32.22393. PMID 10428811.
11. ^ Haendeler J, Yin G, Hojo Y, Saito Y, Melaragno M, Yan C, Sharma VK, Heller M, Aebersold R, Berk BC (December 2003). "GIT1 mediates Src-dependent activation of phospholipase Cgamma by angiotensin II and epidermal growth factor". J. Biol. Chem. 278 (50): 49936–44. doi:10.1074/jbc.M307317200. PMID 14523024.
12. ^ a b c Ko J, Kim S, Valtschanoff JG, Shin H, Lee JR, Sheng M, Premont RT, Weinberg RJ, Kim E (March 2003). "Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting". J. Neurosci. 23 (5): 1667–77. doi:10.1523/JNEUROSCI.23-05-01667.2003. PMC 6741975. PMID 12629171.
13. ^ a b Ko J, Na M, Kim S, Lee JR, Kim E (October 2003). "Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins". J. Biol. Chem. 278 (43): 42377–85. doi:10.1074/jbc.M307561200. PMID 12923177.
14. ^ Zhao ZS, Manser E, Loo TH, Lim L (September 2000). "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly". Mol. Cell. Biol. 20 (17): 6354–63. doi:10.1128/mcb.20.17.6354-6363.2000. PMC 86110. PMID 10938112.

• Hoefen RJ, Berk BC (2006). "The multifunctional GIT family of proteins". J. Cell Sci. 119 (Pt 8): 1469–1475. doi:10.1242/jcs.02925. PMID 16598076.

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.

• Zhao ZS, Manser E, Loo TH, Lim L (2000). "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly". Mol. Cell. Biol. 20 (17): 6354–6363. doi:10.1128/MCB.20.17.6354-6363.2000. PMC 86110. PMID 10938112.

• Kawachi H, Fujikawa A, Maeda N, Noda M (2001). "Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system". Proc. Natl. Acad. Sci. U.S.A. 98 (12): 6593–6598. Bibcode:2001PNAS...98.6593K. doi:10.1073/pnas.041608698. PMC 34398. PMID 11381105.

• Manabe R, Kovalenko M, Webb DJ, Horwitz AR (2002). "GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration". J. Cell Sci. 115 (Pt 7): 1497–510. doi:10.1242/jcs.115.7.1497. PMID 11896197.

• Nishiya N, Shirai T, Suzuki W, Nose K (2003). "Hic-5 interacts with GIT1 with a different binding mode from paxillin". J. Biochem. 132 (2): 279–89. doi:10.1093/oxfordjournals.jbchem.a003222. PMID 12153727.

• Kim S, Ko J, Shin H, Lee JR, Lim C, Han JH, Altrock WD, Garner CC, Gundelfinger ED, Premont RT, Kaang BK, Kim E (2003). "The GIT family of proteins forms multimers and associates with the presynaptic cytomatrix protein Piccolo". J. Biol. Chem. 278 (8): 6291–6300. doi:10.1074/jbc.M212287200. PMID 12473661.

• Shin H, Wyszynski M, Huh KH, Valtschanoff JG, Lee JR, Ko J, Streuli M, Weinberg RJ, Sheng M, Kim E (2003). "Association of the kinesin motor KIF1A with the multimodular protein liprin-alpha". J. Biol. Chem. 278 (13): 11393–11401. doi:10.1074/jbc.M211874200. PMID 12522103.

• Ko J, Kim S, Valtschanoff JG, Shin H, Lee JR, Sheng M, Premont RT, Weinberg RJ, Kim E (2003). "Interaction between liprin-alpha and GIT1 is required for AMPA receptor targeting". J. Neurosci. 23 (5): 1667–77. doi:10.1523/JNEUROSCI.23-05-01667.2003. PMC 6741975. PMID 12629171.

• Ko J, Na M, Kim S, Lee JR, Kim E (2004). "Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins". J. Biol. Chem. 278 (43): 42377–42385. doi:10.1074/jbc.M307561200. PMID 12923177.

• Haendeler J, Yin G, Hojo Y, Saito Y, Melaragno M, Yan C, Sharma VK, Heller M, Aebersold R, Berk BC (2004). "GIT1 mediates Src-dependent activation of phospholipase Cgamma by angiotensin II and epidermal growth factor". J. Biol. Chem. 278 (50): 49936–49944. doi:10.1074/jbc.M307317200. PMID 14523024.

• van Nieuw Amerongen GP, Natarajan K, Yin G, Hoefen RJ, Osawa M, Haendeler J, Ridley AJ, Fujiwara K, van Hinsbergh VW, Berk BC (2004). "GIT1 mediates thrombin signaling in endothelial cells: role in turnover of RhoA-type focal adhesions". Circ. Res. 94 (8): 1041–1049. doi:10.1161/01.RES.0000125627.77235.0C. PMID 15016733.

• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.

• Goehler H, Lalowski M, Stelzl U, Waelter S, Stroedicke M, Worm U, Droege A, Lindenberg KS, Knoblich M, Haenig C, Herbst M, Suopanki J, Scherzinger E, Abraham C, Bauer B, Hasenbank R, Fritzsche A, Ludewig AH, Büssow K, Buessow K, Coleman SH, Gutekunst CA, Landwehrmeyer BG, Lehrach H, Wanker EE (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–865. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.

• GIT1 Info with links in the Cell Migration Gateway Archived 2014-12-11 at the Wayback Machine