RhoD

RHOD
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2J1L
Identifiers
Aliases	RHOD, ARHD, RHOHP1, RHOM, Rho, RhoD, ras homolog family member D
External IDs	OMIM: 605781 MGI: 108446 HomoloGene: 22409 GeneCards: RHOD
Gene location (Human)
Chr.	Chromosome 11 (human)
End	67,072,017 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	4,489,460 bp
RNA expression pattern
	Top expressed in
	Right lobe of liver; ; liver; ; cavity of mouth;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; protein kinase binding; GTP binding; GO:0006184 GTPase activity;
Cellular component	early endosome; endosome membrane; endosome; membrane; cytosol; plasma membrane; intracellular anatomical structure; cytoplasm; cell cortex; cell division site; intracellular membrane-bounded organelle;
Biological process	positive regulation of cell adhesion; focal adhesion assembly; actin filament bundle assembly; regulation of actin cytoskeleton reorganization; positive regulation of cell migration; lamellipodium assembly; Rho protein signal transduction; regulation of focal adhesion assembly; protein targeting; regulation of small GTPase mediated signal transduction; small GTPase mediated signal transduction; actin filament organization; regulation of cell shape; cell migration; regulation of cell migration; establishment or maintenance of actin cytoskeleton polarity; regulation of actin cytoskeleton organization;
	Sources:Amigo / QuickGO
Orthologs
	29984
	11854
	ENSG00000173156
	ENSMUSG00000041845
	O00212
	P97348
	NM_014578; NM_001300886
	NM_007485; NM_001329989
	NP_001287815; NP_055393
	NP_001316918; NP_031511
	Wikidata
View/Edit Human	View/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[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000173156 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000041845 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "Entrez Gene: RHOD ras homolog gene family, member D".
^ 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.
^ 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. S2CID 17891748.

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. S2CID 37763952.
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. S2CID 84584317.
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. doi:10.1523/JNEUROSCI.22-02-00471.2002. PMC 6758682. 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. S2CID 17891748.
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. S2CID 39457788.
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. S2CID 33688226.
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.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by .

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000173156 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000041845 - 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.

[Ridley-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.

[entrezd-6] "Entrez Gene: RHOD ras homolog gene family, member D".

[pmid14749388-7] 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.

[pmid12577064-8] 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. S2CID 17891748.

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