Rnd2

RND2
Identifiers
AliasesRND2, ARHN, RHO7, RhoN, Rnd2, Rho family GTPase 2
External IDsMGI: 1338755 HomoloGene: 21123 GeneCards: RND2
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17q21.31Start43,025,241 bp[1]
End43,032,036 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 11: 101.46 – 101.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

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:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000108830 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001313 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. 1 2 "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. 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. 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.


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