GIT1

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GIT1
Identifiers
Aliases GIT1, GIT ArfGAP 1
External IDs MGI: 1927140 HomoloGene: 32204 GeneCards: GIT1
Gene location (Human)
Chromosome 17 (human)
Chr. Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for GIT1
Genomic location for GIT1
Band 17q11.2 Start 29,573,469 bp[1]
End 29,594,054 bp[1]
RNA expression pattern
PBB GE GIT1 218030 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001085454
NM_014030

NM_001004144

RefSeq (protein)

NP_001078923
NP_054749

NP_001004144

Location (UCSC) Chr 17: 29.57 – 29.59 Mb Chr 11: 77.49 – 77.51 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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]

Interactions[edit]

GIT1 has been shown to interact with:

References[edit]

  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:". 
  4. ^ "Mouse PubMed Reference:". 
  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. doi:10.1073/pnas.95.24.14082. PMC 24330Freely accessible. 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 2172873Freely accessible. 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. 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 86110Freely accessible. PMID 10938112. 

Further reading[edit]

External links[edit]