Rnd1

Rho family GTPase 1
PDB rendering based on 2cls.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2CLS​, 2REX​, 3Q3J​
Identifiers
Symbols	RND1 ; ARHS; RHO6; RHOS
External IDs	OMIM: 609038 MGI: 2444878 HomoloGene: 8706 GeneCards: RND1 Gene
Gene ontology Molecular function • GTPase activity • receptor binding • protein binding • GTP binding Cellular component • cytosol • cytoskeleton • plasma membrane • adherens junction Biological process • actin filament organization • negative regulation of cell adhesion • small GTPase mediated signal transduction • axon guidance • neuron remodeling Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	27289	223881
Ensembl	ENSG00000172602	ENSMUSG00000054855
UniProt	Q92730	Q8BLR7
RefSeq (mRNA)	NM_014470	NM_172612
RefSeq (protein)	NP_055285	NP_766200
Location (UCSC)	Chr 12: 48.86 – 48.87 Mb	Chr 15: 98.66 – 98.68 Mb
PubMed search

Rnd1 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.^[1] It is encoded by the gene RND1.^[2]

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM]^[2]

Interactions

Rnd1 has been shown to interact with GRB7,^[3] PLXNB1,^[4] PDE6D,^[5][6] ARHGAP5^[7] and UBXD5.^[8]

References

1. Ridley AJ (Oct 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends in Cell Biology 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
2. "Entrez Gene: RND1 Rho family GTPase 1".
3. Vayssière B, Zalcman G, Mahé Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J (Feb 2000). "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family". FEBS Letters 467 (1): 91–6. doi:10.1016/S0014-5793(99)01530-6. PMID 10664463.
4. Oinuma I, Katoh H, Harada A, Negishi M (Jul 2003). "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells". The Journal of Biological Chemistry 278 (28): 25671–7. doi:10.1074/jbc.M303047200. PMID 12730235.
5. Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
6. Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
7. 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". Current Biology 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMID 12842009.
8. 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". Molecular and Cellular Biology 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.

Further reading

• Nobes CD, Lauritzen I, Mattei MG, Paris S, Hall A, Chardin P (Apr 1998). "A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion". The Journal of Cell Biology 141 (1): 187–97. doi:10.1083/jcb.141.1.187. PMC 2132722. PMID 9531558.
• Vayssière B, Zalcman G, Mahé Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J (Feb 2000). "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family". FEBS Letters 467 (1): 91–6. doi:10.1016/S0014-5793(99)01530-6. PMID 10664463.
• Aoki J, Katoh H, Mori K, Negishi M (Nov 2000). "Rnd1, a novel rho family GTPase, induces the formation of neuritic processes in PC12 cells". Biochemical and Biophysical Research Communications 278 (3): 604–8. doi:10.1006/bbrc.2000.3842. PMID 11095956.
• Rohm B, Rahim B, Kleiber B, Hovatta I, Püschel AW (Dec 2000). "The semaphorin 3A receptor may directly regulate the activity of small GTPases". FEBS Letters 486 (1): 68–72. doi:10.1016/S0014-5793(00)02240-7. PMID 11108845.
• Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
• 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". Molecular and Cellular Biology 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.
• Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
• Oinuma I, Katoh H, Harada A, Negishi M (Jul 2003). "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells". The Journal of Biological Chemistry 278 (28): 25671–7. doi:10.1074/jbc.M303047200. PMID 12730235.
• Oinuma I, Ishikawa Y, Katoh H, Negishi M (Aug 2004). "The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras". Science 305 (5685): 862–5. doi:10.1126/science.1097545. PMID 15297673.
• Harada A, Katoh H, Negishi M (May 2005). "Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells". The Journal of Biological Chemistry 280 (18): 18418–24. doi:10.1074/jbc.M411356200. PMID 15738000.
• Kim YS, Hori M, Yasuda K, Ozaki H (Dec 2005). "Differences in the gestational pattern of mRNA expression of the Rnd family in rat and human myometria". Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology 142 (4): 410–5. doi:10.1016/j.cbpa.2005.08.028. PMID 16311049.