RhoD

RHOD
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRHOD, ARHD, RHOHP1, RHOM, Rho, RhoD, ras homolog family member D
External IDsMGI: 108446 HomoloGene: 22409 GeneCards: RHOD
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q13.2Start67,056,818 bp[1]
End67,072,013 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

29984

11854

Ensembl

ENSG00000173156

ENSMUSG00000041845

UniProt

O00212

P97348

RefSeq (mRNA)

NM_014578
NM_001300886

NM_007485
NM_001329989

RefSeq (protein)

NP_001287815
NP_055393

NP_001316918
NP_031511

Location (UCSC)Chr 11: 67.06 – 67.07 MbChr 19: 4.43 – 4.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

RhoD (Ras homolog gene family, member D) 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.[5] It is encoded by the gene RHOD.[6]

It binds GTP and is involved in endosome dynamics and reorganization of the actin cytoskeleton, and it may coordinate membrane transport with the function of the cytoskeleton.[6]

Interactions

RhoD has been shown to interact with CNKSR1[7] and DIAPH2.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000173156 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041845 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. ISSN 0962-8924. PMID 16949823.
  6. 1 2 "Entrez Gene: RHOD ras homolog gene family, member D".
  7. ↑ Jaffe, Aron B; Aspenström Pontus; Hall Alan (Feb 2004). "Human CNK1 Acts as a Scaffold Protein, Linking Rho and Ras Signal Transduction Pathways". Mol. Cell. Biol. United States. 24 (4): 1736–46. doi:10.1128/MCB.24.4.1736-1746.2004. ISSN 0270-7306. PMC 344169. PMID 14749388.
  8. ↑ Gasman, Stéphane; Kalaidzidis Yannis; Zerial Marino (Mar 2003). "RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase". Nat. Cell Biol. England. 5 (3): 195–204. doi:10.1038/ncb935. ISSN 1465-7392. PMID 12577064.

Further reading

  • Ridley AJ (2001). "Rho proteins: linking signaling with membrane trafficking". Traffic. 2 (5): 303–10. doi:10.1034/j.1600-0854.2001.002005303.x. PMID 11350626.
  • Shimizu F, Watanabe TK, Okuno S, et al. (1997). "Isolation of a novel human cDNA (rhoHP1) homologous to rho genes". Biochim. Biophys. Acta. 1351 (1–2): 13–6. doi:10.1016/s0167-4781(97)00008-0. PMID 9116026.
  • Kim HS, Choi JY, Jung AR, et al. (2000). "Assignment of the human RhoHP1 gene (ARHD) to chromosome 11q14.3 by radiation hybrid mapping". Cytogenet. Cell Genet. 89 (1–2): 53. doi:10.1159/000015562. PMID 10894936.
  • Murphy C, Saffrich R, Olivo-Marin JC, et al. (2001). "Dual function of rhoD in vesicular movement and cell motility". Eur. J. Cell Biol. 80 (6): 391–8. doi:10.1078/0171-9335-00173. PMID 11484930.
  • Zanata SM, Hovatta I, Rohm B, Püschel AW (2002). "Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse". J. Neurosci. 22 (2): 471–7. PMID 11784792.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gasman S, Kalaidzidis Y, Zerial M (2003). "RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase". Nat. Cell Biol. 5 (3): 195–204. doi:10.1038/ncb935. PMID 12577064.
  • Jaffe AB, Aspenström P, Hall A (2004). "Human CNK1 Acts as a Scaffold Protein, Linking Rho and Ras Signal Transduction Pathways". Mol. Cell. Biol. 24 (4): 1736–46. doi:10.1128/MCB.24.4.1736-1746.2004. PMC 344169. PMID 14749388.
  • Flaxenburg JA, Melter M, Lapchak PH, et al. (2004). "The CD40-induced signaling pathway in endothelial cells resulting in the overexpression of vascular endothelial growth factor involves Ras and phosphatidylinositol 3-kinase". J. Immunol. 172 (12): 7503–9. doi:10.4049/jimmunol.172.12.7503. PMID 15187129.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153.
  • Birukova AA, Chatchavalvanich S, Rios A, et al. (2006). "Differential Regulation of Pulmonary Endothelial Monolayer Integrity by Varying Degrees of Cyclic Stretch". Am. J. Pathol. 168 (5): 1749–61. doi:10.2353/ajpath.2006.050431. PMC 1606576. PMID 16651639.
  • Ito Y, Kanamaru A, Tada A (2007). "A novel agent, methylophiopogonanone B, promotes Rho activation and tubulin depolymerization". Mol. Cell. Biochem. 297 (1–2): 121–9. doi:10.1007/s11010-006-9336-y. PMID 17029007.
  • Tan W, Martin D, Gutkind JS (2007). "The Galpha13-Rho signaling axis is required for SDF-1-induced migration through CXCR4". J. Biol. Chem. 281 (51): 39542–9. doi:10.1074/jbc.M609062200. PMID 17056591.
  • Lakshman N, Kim A, Bayless KJ, et al. (2007). "Rho plays a central role in regulating local cell-matrix mechanical interactions in 3D culture". Cell Motil. Cytoskeleton. 64 (6): 434–45. doi:10.1002/cm.20194. PMID 17342762.


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