ARHGDIA

Rho GDP-dissociation inhibitor 1 is a protein that in humans is encoded by the ARHGDIA gene.[5][6]

ARHGDIA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CC0, 1FSO, 1FST, 1FT0, 1FT3, 1HH4, 1KMT, 1QVY, 1RHO, 2BXW, 2JHS, 2JHT, 2JHU, 2JHV, 2JHW, 2JHX, 2JHY, 2JHZ, 2JI0, 2N80
Identifiers
Aliases	ARHGDIA, GDIA1, HEL-S-47e, NPHS8, RHOGDI, RHOGDI-1, Rho GDP dissociation inhibitor alpha
External IDs	OMIM: 601925 MGI: 2178103 HomoloGene: 908 GeneCards: ARHGDIA
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q25.3 Start 81,867,721 bp[1] End 81,871,378 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 E2 Start 120,578,104 bp[2] End 120,581,624 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • Rho GDP-dissociation inhibitor activity • GO:0001948 protein binding • Rac GTPase binding Cellular component • cytoplasm • cytosol • extracellular exosome • cytoskeleton • membrane Biological process • negative regulation of cell adhesion • regulation of actin cytoskeleton reorganization • movement of cell or subcellular component • negative regulation of apoptotic process • positive regulation of axonogenesis • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • negative regulation of axonogenesis • regulation of Rho protein signal transduction • regulation of small GTPase mediated signal transduction • semaphorin-plexin signaling pathway • GO:0048552 regulation of catalytic activity • Rho protein signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	396	192662
Ensembl	ENSG00000141522	ENSMUSG00000025132
UniProt	P52565	Q99PT1
RefSeq (mRNA)	NM_001185077 NM_001185078 NM_001301240 NM_001301241 NM_001301242 NM_001301243 NM_004309	NM_133796 NM_001363425
RefSeq (protein)	NP_001172006 NP_001172007 NP_001288169 NP_001288170 NP_001288171 NP_001288172 NP_004300	NP_598557 NP_001350354
Location (UCSC)	Chr 17: 81.87 – 81.87 Mb	Chr 11: 120.58 – 120.58 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

ARHGDIA has been shown to interact with:

• CDC42,[7][8]
• RAC1,[7][8][9][10][11][12]
• RHOA,[7][8][9][13][14]
• Rac2,[8][9] and
• RhoH.[9][15]

References

1. GRCh38: Ensembl release 89: ENSG00000141522 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025132 - 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. 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. doi:10.1159/000134538. PMID 9186513.
6. "Entrez Gene: ARHGDIA Rho GDP dissociation inhibitor (GDI) alpha".
7. 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
8. 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. doi:10.1016/s0014-5793(98)00020-9. PMID 9490022.
9. Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/s0300-9084(01)01263-9. PMID 11368848.
10. 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. doi:10.1021/bi010288k. PMID 11513578.
11. 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. doi:10.1016/s0969-2126(00)00080-0. PMID 10673424.
12. 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. doi:10.1021/bi010289c. PMID 11513579.
13. 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. doi:10.1074/jbc.M411781200. PMID 15659383.
14. 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. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
15. 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. doi:10.1128/mcb.22.4.1158-1171.2002. PMC 134637. PMID 11809807.

External links

• Human ARHGDIA genome location and ARHGDIA gene details page in the UCSC Genome Browser.

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. doi:10.1006/excr.1993.1298. PMID 8262133.
• 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. doi:10.1016/S0969-2126(97)00218-9. PMID 9195882.
• 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. doi:10.1074/jbc.272.37.23371. PMID 9287351.
• 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. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022.
• 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. doi:10.1038/sj.onc.1201874. PMID 9681826.
• 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. doi:10.1021/bi9829837. PMID 10346909.
• 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. doi:10.1016/S0014-5793(00)01121-2. PMID 10664460.
• 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. doi:10.1016/S0969-2126(00)00080-0. PMID 10673424.
• 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. doi:10.1016/S0092-8674(00)80670-4. PMID 10676816.
• 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. doi:10.1038/sj.cdd.4400616. PMID 10713718.
• 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. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
• 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. doi:10.1107/S0907444901003122. PMID 11320308.
• 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. doi:10.1021/bi010288k. PMID 11513578.
• 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. doi:10.1021/bi010289c. PMID 11513579.
• DerMardirossian C, Schnelzer A, Bokoch GM (2004). "Phosphorylation of RhoGDI by Pak1 mediates dissociation of Rac GTPase". Mol. Cell. 15 (1): 117–27. doi:10.1016/j.molcel.2004.05.019. PMID 15225553.
• 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. doi:10.1074/jbc.M409741200. PMID 15513926.
• 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. doi:10.1074/jbc.M411781200. PMID 15659383.