Rnd2

RND2
Identifiers
Aliases	RND2 , ARHN, RHO7, RhoN, Rnd2, Rho family GTPase 2
External IDs	OMIM: 601555; MGI: 1338755; HomoloGene: 21123; GeneCards: RND2; OMA:RND2 - orthologs
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 101,355,825 bp [2] End 101,362,679 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in C1 segment internal globus pallidus hypothalamus substantia nigra superior vestibular nucleus nucleus accumbens pars reticulata left testis external globus pallidus right testis Top expressed in ganglionic eminence cerebellar cortex pons inferior colliculi medulla oblongata striatum of neuraxis superior frontal gyrus superior colliculus olfactory bulb dentate gyrus of hippocampal formation granule cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GTP binding protein binding GTPase activity protein N-terminus binding protein kinase binding Cellular component early endosome acrosomal membrane membrane cytoplasmic vesicle intracellular anatomical structure cytoplasm plasma 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: 101.36 – 101.36 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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:

• 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. Bibcode:2003CBio...13.1106W. 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. S2CID   4427026.
• 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. A. 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.