RhoD

Ras homolog family member D
PDB rendering based on 2j1l.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2J1L​
Identifiers
Symbols	RHOD ; ARHD; RHOHP1; RHOM; Rho
External IDs	OMIM: 605781 MGI: 108446 HomoloGene: 22409 GeneCards: RHOD Gene
Gene ontology Molecular function • GTPase activity • GTP binding • protein kinase binding Cellular component • early endosome • cytosol • plasma membrane • endosome membrane Biological process • protein targeting • small GTPase mediated signal transduction • Rho protein signal transduction • lamellipodium assembly • positive regulation of cell migration • positive regulation of cell adhesion • focal adhesion assembly • actin filament bundle assembly • regulation of small GTPase mediated signal transduction • regulation of focal adhesion assembly • regulation of actin cytoskeleton reorganization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	29984	11854
Ensembl	ENSG00000173156	ENSMUSG00000041845
UniProt	O00212	P97348
RefSeq (mRNA)	NM_001300886	NM_007485
RefSeq (protein)	NP_001287815	NP_031511
Location (UCSC)	Chr 11: 67.06 – 67.07 Mb	Chr 19: 4.43 – 4.44 Mb
PubMed search

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.^[1] It is encoded by the gene RHOD.^[2]

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.^[2]

Interactions

RhoD has been shown to interact with CNKSR1^[3] and DIAPH2.^[4]

References

1. 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.
2. "Entrez Gene: RHOD ras homolog gene family, member D".
3. 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.
4. 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. 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. 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.