RhoG

From Wikipedia, the free encyclopedia


Ras homolog gene family, member G (rho G)
Identifiers
Symbol(s) RHOG; ARHG; MGC125835; MGC125836
External IDs OMIM: 179505 MGI1928370 HomoloGene68196
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 391 56212
Ensembl ENSG00000177105 ENSMUSG00000073982
Uniprot P84095 Q3UDZ1
Refseq NM_001665 (mRNA)
NP_001656 (protein)
NM_019566 (mRNA)
NP_062512 (protein)
Location Chr 11: 3.8 - 3.82 Mb Chr 7: 102.11 - 102.11 Mb
Pubmed search [1] [2]

RhoG (Ras homolog gene family, member G) (or ARGH) is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.[1] It is encoded by the gene RHOG.[2]

It acts in the pathway of signal transduction and plays a key role in the regulation of cellular functions.[supplied by OMIM][2]

[edit] References

  1. ^ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol 16 (10): 522-9. ISSN 0962-8924. 
  2. ^ a b Entrez Gene: RHOG ras homolog gene family, member G (rho G).

[edit] Further reading

  • Vincent S, Jeanteur P, Fort P (1992). "Growth-regulated expression of rhoG, a new member of the ras homolog gene family.". Mol. Cell. Biol. 12 (7): 3138-48. PMID 1620121. 
  • Taviaux SA, Vincent S, Fort P, Demaille JG (1993). "Localization of ARHG, a member of the RAS homolog gene family, to 11p15.5-11p15.4 by fluorescence in situ hybridization.". Genomics 16 (3): 788-90. doi:10.1006/geno.1993.1271. PMID 8325658. 
  • Miki T, Smith CL, Long JE, et al. (1993). "Oncogene ect2 is related to regulators of small GTP-binding proteins.". Nature 362 (6419): 462-5. doi:10.1038/362462a0. PMID 8464478. 
  • Zalcman G, Closson V, Camonis J, et al. (1997). "RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG.". J. Biol. Chem. 271 (48): 30366-74. PMID 8939998. 
  • Le Gallic L, Fort P (1997). "Structure of the human ARHG locus encoding the Rho/Rac-like RhoG GTPase.". Genomics 42 (1): 157-60. PMID 9177787. 
  • Gauthier-Rouvière C, Vignal E, Mériane M, et al. (1998). "RhoG GTPase controls a pathway that independently activates Rac1 and Cdc42Hs.". Mol. Biol. Cell 9 (6): 1379-94. PMID 9614181. 
  • Movilla N, Bustelo XR (1999). "Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins.". Mol. Cell. Biol. 19 (11): 7870-85. PMID 10523675. 
  • Matarrese P, Conti L, Varano B, et al. (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. 
  • Vignal E, Blangy A, Martin M, et al. (2001). "Kinectin is a key effector of RhoG microtubule-dependent cellular activity.". Mol. Cell. Biol. 21 (23): 8022-34. doi:10.1128/MCB.21.23.8022-8034.2001. PMID 11689693. 
  • Booden MA, Campbell SL, Der CJ (2002). "Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation.". Mol. Cell. Biol. 22 (8): 2487-97. PMID 11909943. 
  • Wennerberg K, Ellerbroek SM, Liu RY, et al. (2003). "RhoG signals in parallel with Rac1 and Cdc42.". J. Biol. Chem. 277 (49): 47810-7. doi:10.1074/jbc.M203816200. PMID 12376551. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Vigorito E, Billadeu DD, Savoy D, et al. (2003). "RhoG regulates gene expression and the actin cytoskeleton in lymphocytes.". Oncogene 22 (3): 330-42. doi:10.1038/sj.onc.1206116. PMID 12545154. 
  • Katoh H, Negishi M (2003). "RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo.". Nature 424 (6947): 461-4. doi:10.1038/nature01817. PMID 12879077. 
  • Skowronek KR, Guo F, Zheng Y, Nassar N (2004). "The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids.". J. Biol. Chem. 279 (36): 37895-907. doi:10.1074/jbc.M312677200. PMID 15199069. 
  • deBakker CD, Haney LB, Kinchen JM, et al. (2005). "Phagocytosis of apoptotic cells is regulated by a UNC-73/TRIO-MIG-2/RhoG signaling module and armadillo repeats of CED-12/ELMO.". Curr. Biol. 14 (24): 2208-16. doi:10.1016/j.cub.2004.12.029. PMID 15620647. 
  • Katoh H, Hiramoto K, Negishi M (2006). "Activation of Rac1 by RhoG regulates cell migration.". J. Cell. Sci. 119 (Pt 1): 56-65. doi:10.1242/jcs.02720. PMID 16339170. 
  • Prieto-Sánchez RM, Berenjeno IM, Bustelo XR (2006). "Involvement of the Rho/Rac family member RhoG in caveolar endocytosis.". Oncogene 25 (21): 2961-73. doi:10.1038/sj.onc.1209333. PMID 16568096. 
  • Condliffe AM, Webb LM, Ferguson GJ, et al. (2006). "RhoG regulates the neutrophil NADPH oxidase.". J. Immunol. 176 (9): 5314-20. PMID 16621998. 
  • Hiramoto K, Negishi M, Katoh H (2007). "Dock4 is regulated by RhoG and promotes Rac-dependent cell migration.". Exp. Cell Res. 312 (20): 4205-16. doi:10.1016/j.yexcr.2006.09.006. PMID 17027967.