Rnd3

Rnd3 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases.[5] It is encoded by the gene RND3.[6]

RND3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1M7B, 2V55, 4BG6
Identifiers
Aliases	RND3, ARHE, Rho8, RhoE, memB, Rnd3, Rho family GTPase 3
External IDs	OMIM: 602924 MGI: 1921444 HomoloGene: 21074 GeneCards: RND3
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q23.3 Start 150,468,195 bp[1] End 150,539,011 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 C1.1 Start 51,130,438 bp[2] End 51,149,111 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • GO:0001948 protein binding • GTPase activity • protein kinase binding Cellular component • Golgi membrane • Golgi apparatus • extracellular exosome • membrane • focal adhesion • intracellular • cytoplasm • cell membrane • cell cortex • cell division site • intracellular membrane-bounded organelle Biological process • small GTPase mediated signal transduction • cell adhesion • actin cytoskeleton organization • actin filament organization • Rho protein signal transduction • regulation of cell shape • regulation of cell migration • establishment or maintenance of actin cytoskeleton polarity • regulation of actin cytoskeleton organization • actin filament bundle assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	390	74194
Ensembl	ENSG00000115963	ENSMUSG00000017144
UniProt	P61587	P61588
RefSeq (mRNA)	NM_005168 NM_001254738	NM_028810
RefSeq (protein)	NP_001241667 NP_005159	NP_083086
Location (UCSC)	Chr 2: 150.47 – 150.54 Mb	Chr 2: 51.13 – 51.15 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Like other members of the Rho family of Ras-related GTPases it regulates the organization of the actin cytoskeleton in response to extracellular growth factors.

Regulation

Like Ras, Rho family members appear to cycle between an inactive GDP-bound form and an active GTP-bound form. Three major regulators of Rho activity have been identified: RhoGDIs, which interact with the GDP-bound Rho proteins to keep them in a resting complex (see MIM 601925); GEFs, which promote GDP/GTP exchange leading to activation of Rho proteins (see MIM 601855); and GAPs, which stimulate GTP hydrolysis and return the activated Rho protein to its inactive form (see MIM 602680) (Nobes et al., 1998).[supplied by OMIM][6]

Interactions

Rnd3 has been shown to interact with ARHGAP5[7] and UBXD5.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000115963 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000017144 - 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. 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. PMID 16949823.
6. "Entrez Gene: RND3 Rho family GTPase 3".
7. Wennerberg, Krister; Forget Marie-Annick; Ellerbroek Shawn M; Arthur William T; Burridge Keith; Settleman Jeffrey; Der Channing J; Hansen Steen H (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. ISSN 0960-9822. PMC 6918695. PMID 12842009.
8. Katoh, Hironori; Harada Amane; Mori Kazutoshi; Negishi Manabu (May 2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Mol. Cell. Biol. 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. ISSN 0270-7306. PMC 133765. PMID 11940653.

Further reading

• Foster R, Hu KQ, Lu Y, et al. (1996). "Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation". Mol. Cell. Biol. 16 (6): 2689–99. doi:10.1128/MCB.16.6.2689. PMC 231259. PMID 8649376.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Nobes CD, Lauritzen I, Mattei MG, et al. (1998). "A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion". J. Cell Biol. 141 (1): 187–97. doi:10.1083/jcb.141.1.187. PMC 2132722. PMID 9531558.
• Katoh H, Harada A, Mori K, Negishi M (2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Mol. Cell. Biol. 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.
• Fiegen D, Blumenstein L, Stege P, et al. (2002). "Crystal structure of Rnd3/RhoE: functional implications". FEBS Lett. 525 (1–3): 100–4. doi:10.1016/S0014-5793(02)03094-6. PMID 12163169.
• 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.
• Riento K, Guasch RM, Garg R, et al. (2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. PMC 156133. PMID 12773565.
• Wennerberg K, Forget MA, Ellerbroek SM, et al. (2004). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMC 6918695. PMID 12842009.
• 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.
• Bektic J, Pfeil K, Berger AP, et al. (2005). "Small G-protein RhoE is underexpressed in prostate cancer and induces cell cycle arrest and apoptosis". Prostate. 64 (4): 332–40. doi:10.1002/pros.20243. PMID 15754346.
• Rubenstein NM, Chan JF, Kim JY, et al. (2005). "Rnd3/RhoE induces tight junction formation in mammary epithelial tumor cells". Exp. Cell Res. 305 (1): 74–82. doi:10.1016/j.yexcr.2004.12.010. PMID 15777789.
• Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
• Kim YS, Hori M, Yasuda K, Ozaki H (2006). "Differences in the gestational pattern of mRNA expression of the Rnd family in rat and human myometria". Comp. Biochem. Physiol., Part a Mol. Integr. Physiol. 142 (4): 410–5. doi:10.1016/j.cbpa.2005.08.028. PMID 16311049.
• Ongusaha PP, Kim HG, Boswell SA, et al. (2007). "RhoE is a pro-survival p53 target gene that inhibits ROCK I-mediated apoptosis in response to genotoxic stress". Curr. Biol. 16 (24): 2466–72. doi:10.1016/j.cub.2006.10.056. PMC 2779528. PMID 17174923.
• Poch E, Miñambres R, Mocholí E, et al. (2007). "RhoE interferes with Rb inactivation and regulates the proliferation and survival of the U87 human glioblastoma cell line". Exp. Cell Res. 313 (4): 719–31. doi:10.1016/j.yexcr.2006.11.006. PMID 17182035.