GIT1

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

GIT1
Identifiers
AliasesGIT1, GIT ArfGAP 1, p95-APP1
External IDsOMIM: 608434 MGI: 1927140 HomoloGene: 32204 GeneCards: GIT1
Orthologs
SpeciesHumanMouse
Entrez

28964

216963

Ensembl

ENSG00000108262

ENSMUSG00000011877

UniProt

Q9Y2X7

Q68FF6

RefSeq (mRNA)

NM_001085454
NM_014030

NM_001004144
NM_001374758

RefSeq (protein)

NP_001078923
NP_054749

NP_001004144
NP_001361687

Location (UCSC)Chr 17: 29.57 – 29.59 MbChr 11: 77.38 – 77.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

Interactions

GIT1 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000108262 - Ensembl, May 2017
  2. 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. 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. 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. 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. 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. 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.

Further reading


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