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Ras homolog gene family, member A
PDB rendering based on 1a2b.
Available structures
1a2b, 1cc0, 1cxz, 1dpf, 1ftn, 1kmq, 1lb1, 1ow3, 1s1c, 1tx4, 1x86, 1xcg, 1z2c, 2gcn, 2gco, 2gcp
Identifiers
Symbols	RHOA; ARH12; ARHA; RHO12; RHOH12
External IDs	OMIM: 165390 MGI: 1096342 HomoloGene: 1257 GeneCards: RHOA Gene
Gene ontology Molecular function • nucleotide binding • magnesium ion binding • GTPase activity • signal transducer activity • protein binding • GTP binding Cellular component • intracellular • cytoskeleton • membrane Biological process • small GTPase mediated signal transduction • Rho protein signal transduction • actin cytoskeleton organization and biogenesis • positive regulation of NF-kappaB import into nucleus • positive regulation of I-kappaB kinase/NF-kappaB cascade
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	387	11848
Ensembl	ENSG00000067560	ENSMUSG00000007815
UniProt	P61586	Q3TN61
RefSeq (mRNA)	NM_001664	NM_016802
RefSeq (protein)	NP_001655	NP_058082
Location (UCSC)	Chr 3: 49.37 - 49.42 Mb	Chr 9: 108.16 - 108.2 Mb
PubMed search	[1]	[2]

Ras homolog gene family, member A (RhoA) is a small GTPase protein known to regulate the actin cytoskeleton in the formation of stress fibers. It is encoded by the gene RHOA.

It acts upon two known effector proteins: ROCK1 (Rho-associated, coiled-coil containing protein kinase 1) and DIAPH1 (diaphanous homolog 1 (Drosophila)).

RhoA is part of a larger family of related proteins known as the Ras superfamily; proteins involved in the regulation and timing of cell division.

RhoA Pathway

Molecules act on various receptors, such as NgR1, LINGO1, p75, TROY and other unknown receptors (eg. by CSPGs), which stimulates RhoA. RhoA activates ROCK (RhoA kinase) which stimulates LIM kinase, which then stimulates Cofilin, which effectively re-organises the Actin cytoskeleton of the cell¹. In the case of neurons, activation of this pathway results in growth cone collapse,^1,3 therefore inhibits the growth and repair of neural pathways and axons. Inhibition of this pathway by its various components usually results in some level of improved remyelination.^[1][2][3][4]

Interactions

RHOA has been shown to interact with Phospholipase D1,^[5][6] PLCG1,^[7] ARHGAP5,^[8] ARHGAP1,^{[9][10][11][12]} TRPC1,^[13] ITPR1,^[13] DIAPH1,^[14] GEFT,^[15] ARHGEF3,^[16] ARHGEF12,^[17][18] ARHGDIA,^{[19][20][21][22][23]} KCNA2,^[24] RAP1GDS1,^[25] DGKQ,^[26] TRIO,^[27] ROCK1,^[14][28][29] ARHGEF11,^[30] RICS,^[31][32][33] PKN2,^[34][35] M-RIP,^[36] Protein kinase N1,^[14][37][35] CIT^[14][38] and KTN1.^{[14][39][40][41]}

References

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Further reading

PDB Gallery 1a2b: HUMAN RHOA COMPLEXED WITH GTP ANALOGUE   1cc0: CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX   1cxz: CRYSTAL STRUCTURE OF HUMAN RHOA COMPLEXED WITH THE EFFECTOR DOMAIN OF THE PROTEIN KINASE PKN/PRK1   1dpf: CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP   1ftn: CRYSTAL STRUCTURE OF THE HUMAN RHOA/GDP COMPLEX   1kmq: Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)   1lb1: Crystal Structure of the Dbl and Pleckstrin homology domains of Dbs in complex with RhoA   1ow3: Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP   1s1c: Crystal structure of the complex between the human RhoA and Rho-binding domain of human ROCKI   1tx4: RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX   1x86: Crystal Structure of the DH/PH domains of Leukemia-associated RhoGEF in complex with RhoA   1xcg: Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF   1z2c: Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP   2gcn: Crystal structure of the human RhoC-GDP complex   2gco: Crystal structure of the human RhoC-GppNHp complex   2gcp: Crystal structure of the human RhoC-GSP complex

Notes

External links

• MeSH rhoA+Protein