Rnd2

Rnd2 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 RND2.[6]

RND2
Identifiers
Aliases	RND2, ARHN, RHO7, RhoN, Rnd2, Rho family GTPase 2
External IDs	OMIM: 601555 MGI: 1338755 HomoloGene: 21123 GeneCards: RND2
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.31 Start 43,025,231 bp[1] End 43,032,041 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 D Start 101,464,999 bp[2] End 101,471,853 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • GO:0001948 protein binding • GTPase activity • protein N-terminus binding • protein kinase binding Cellular component • early endosome • acrosomal membrane • membrane • cytoplasmic vesicle • intracellular • cytoplasm • cell membrane • cell cortex • cell division site • intracellular membrane-bounded organelle Biological process • small GTPase mediated signal transduction • positive regulation of collateral sprouting • signal transduction • 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	8153	11858
Ensembl	ENSG00000108830	ENSMUSG00000001313
UniProt	P52198	Q9QYM5
RefSeq (mRNA)	NM_005440	NM_009708
RefSeq (protein)	NP_005431	NP_033838
Location (UCSC)	Chr 17: 43.03 – 43.03 Mb	Chr 11: 101.46 – 101.47 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM][7]

This particular family member has been implicated in the regulation of neuronal morphology and endosomal trafficking.

Clinical significance

The gene localizes to chromosome 17 and is the centromeric neighbor of the breast-ovarian cancer susceptibility gene BRCA1.[6]

Interactions

Rnd2 has been shown to interact with:

• ARHGAP5,[8]
• RACGAP1,[9] and
• UBXD5.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000108830 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001313 - 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 AJ (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. "Entrez Gene: RND2 Rho family GTPase 2".
7. "Entrez Gene: RND1 Rho family GTPase 1".
8. Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (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. PMC 6918695. PMID 12842009.
9. Naud N, Touré A, Liu J, Pineau C, Morin L, Dorseuil O, Escalier D, Chardin P, Gacon G (May 2003). "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells". Biochem. J. 372 (Pt 1): 105–12. doi:10.1042/BJ20021652. PMC 1223378. PMID 12590651.
10. Katoh H, Harada A, Mori K, Negishi M (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. PMC 133765. PMID 11940653.

Further reading

• Chardin P (1991). "Small GTP-binding proteins of the ras family: a conserved functional mechanism?". Cancer Cells. 3 (4): 117–26. PMID 1909153.
• 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.
• Smith TM, Lee MK, Szabo CI, Jerome N, McEuen M, Taylor M, Hood L, King MC (1997). "Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1". Genome Res. 6 (11): 1029–49. doi:10.1101/gr.6.11.1029. PMID 8938427.
• Nobes CD, Lauritzen I, Mattei MG, Paris S, Hall A, Chardin P (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.
• Tanaka H, Fujita H, Katoh H, Mori K, Negishi M (2002). "Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2". Biochem. J. 365 (Pt 2): 349–53. doi:10.1042/BJ20020062. PMC 1222680. PMID 11931639.
• 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.
• Fujita H, Katoh H, Ishikawa Y, Mori K, Negishi M (2003). "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching". J. Biol. Chem. 277 (47): 45428–34. doi:10.1074/jbc.M208090200. PMID 12244061.
• Naud N, Touré A, Liu J, Pineau C, Morin L, Dorseuil O, Escalier D, Chardin P, Gacon G (2003). "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells". Biochem. J. 372 (Pt 1): 105–12. doi:10.1042/BJ20021652. PMC 1223378. PMID 12590651.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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.
• Tanaka H, Katoh H, Negishi M (2006). "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity". J. Biol. Chem. 281 (15): 10355–64. doi:10.1074/jbc.M511314200. PMID 16481321.