ARHGDIA

ARHGDIA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARHGDIA, GDIA1, HEL-S-47e, NPHS8, RHOGDI, RHOGDI-1, Rho GDP dissociation inhibitor alpha
External IDsMGI: 2178103 HomoloGene: 908 GeneCards: ARHGDIA
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

396

192662

Ensembl

ENSG00000141522

ENSMUSG00000025132

UniProt

P52565

Q99PT1

RefSeq (mRNA)

NM_133796

RefSeq (protein)

NP_598557

Location (UCSC)Chr 17: 81.87 – 81.87 MbChr 11: 120.58 – 120.58 Mb
PubMed search[1][2]
Wikidata
View/Edit HumanView/Edit Mouse

Rho GDP-dissociation inhibitor 1 is a protein that in humans is encoded by the ARHGDIA gene.[3][4]

Interactions

ARHGDIA has been shown to interact with:

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Wagner T, Tommerup N, Wirth J, Leffers H, Zimmer J, Back E, Weissenbach J, Scherer G (July 1997). "A somatic cell hybrid panel for distal 17q: GDIA1 maps to 17q25.3". Cytogenet Cell Genet. 76 (3–4): 172–5. PMID 9186513. doi:10.1159/000134538.
  4. ↑ "Entrez Gene: ARHGDIA Rho GDP dissociation inhibitor (GDI) alpha".
  5. 1 2 3 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. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. PMC 1847948 Freely accessible. PMID 17353931. doi:10.1038/msb4100134.
  6. 1 2 3 4 Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. PMID 9490022. doi:10.1016/s0014-5793(98)00020-9.
  7. 1 2 3 4 Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. PMID 11368848. doi:10.1016/s0300-9084(01)01263-9.
  8. ↑ Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (August 2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. PMID 11513578. doi:10.1021/bi010288k.
  9. ↑ Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (January 2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. PMID 10673424. doi:10.1016/s0969-2126(00)00080-0.
  10. ↑ Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (August 2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. PMID 11513579. doi:10.1021/bi010289c.
  11. ↑ Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. PMID 15659383. doi:10.1074/jbc.M411781200.
  12. ↑ Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (January 2001). "Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding". J. Cell Biol. 152 (1): 111–26. PMC 2193662 Freely accessible. PMID 11149925. doi:10.1083/jcb.152.1.111.
  13. ↑ Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Mol. Cell. Biol. 22 (4): 1158–71. PMC 134637 Freely accessible. PMID 11809807. doi:10.1128/mcb.22.4.1158-1171.2002.

Further reading

  • Leffers H, Nielsen MS, Andersen AH, Honoré B, Madsen P, Vandekerckhove J, Celis JE (1994). "Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton". Exp. Cell Res. 209 (2): 165–74. PMID 8262133. doi:10.1006/excr.1993.1298. 
  • Keep NH, Barnes M, Barsukov I, Badii R, Lian LY, Segal AW, Moody PC, Roberts GC (1997). "A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm". Structure. 5 (5): 623–33. PMID 9195882. doi:10.1016/S0969-2126(97)00218-9. 
  • Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y (1997). "Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein". J. Biol. Chem. 272 (37): 23371–5. PMID 9287351. doi:10.1074/jbc.272.37.23371. 
  • Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. PMID 9490022. doi:10.1016/S0014-5793(98)00020-9. 
  • Takahashi K, Sasaki T, Mammoto A, Hotta I, Takaishi K, Imamura H, Nakano K, Kodama A, Takai Y (1998). "Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl". Oncogene. 16 (25): 3279–84. PMID 9681826. doi:10.1038/sj.onc.1201874. 
  • Newcombe AR, Stockley RW, Hunter JL, Webb MR (1999). "The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI". Biochemistry. 38 (21): 6879–86. PMID 10346909. doi:10.1021/bi9829837. 
  • Groysman M, Russek CS, Katzav S (2000). "Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation". FEBS Lett. 467 (1): 75–80. PMID 10664460. doi:10.1016/S0014-5793(00)01121-2. 
  • Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. PMID 10673424. doi:10.1016/S0969-2126(00)00080-0. 
  • Hoffman GR, Nassar N, Cerione RA (2000). "Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI". Cell. 100 (3): 345–56. PMID 10676816. doi:10.1016/S0092-8674(00)80670-4. 
  • Matarrese P, Conti L, Varano B, Gauzzi MC, Belardelli F, Gessani S, Malorni W (2000). "The HIV-1 vpr protein induces anoikis-resistance by modulating cell adhesion process and microfilament system assembly". Cell Death Differ. 7 (1): 25–36. PMID 10713718. doi:10.1038/sj.cdd.4400616. 
  • Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (2001). "Differential Localization of Rho Gtpases in Live Cells: Regulation by Hypervariable Regions and Rhogdi Binding". J. Cell Biol. 152 (1): 111–26. PMC 2193662 Freely accessible. PMID 11149925. doi:10.1083/jcb.152.1.111. 
  • Longenecker KL, Garrard SM, Sheffield PJ, Derewenda ZS (2001). "Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI". Acta Crystallogr. D. 57 (Pt 5): 679–88. PMID 11320308. doi:10.1107/S0907444901003122. 
  • Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. PMID 11513578. doi:10.1021/bi010288k. 
  • Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. PMID 11513579. doi:10.1021/bi010289c. 
  • DerMardirossian C, Schnelzer A, Bokoch GM (2004). "Phosphorylation of RhoGDI by Pak1 mediates dissociation of Rac GTPase". Mol. Cell. 15 (1): 117–27. PMID 15225553. doi:10.1016/j.molcel.2004.05.019. 
  • Dransart E, Morin A, Cherfils J, Olofsson B (2005). "Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors". J. Biol. Chem. 280 (6): 4674–83. PMID 15513926. doi:10.1074/jbc.M409741200. 
  • Gajate C, Mollinedo F (2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. PMID 15659383. doi:10.1074/jbc.M411781200. 
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