4f38

Structural highlights

Function

RHOA_MOUSE Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (PubMed:14697203). Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (By similarity). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:11777936, PubMed:20974804). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center (By similarity). May be an activator of PLCE1 (PubMed:9635436). In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (PubMed:14697203).[UniProtKB:P61586][UniProtKB:P61589]^{[1] [2] [3] [4]}

See Also

• Guanine nucleotide dissociation inhibitor
• Rho GTPase 3D structures

References

1. ↑ Calautti E, Grossi M, Mammucari C, Aoyama Y, Pirro M, Ono Y, Li J, Dotto GP. Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion. J Cell Biol. 2002 Jan 7;156(1):137-48. Epub 2002 Jan 3. PMID:11777936 doi:http://dx.doi.org/10.1083/jcb.200105140
2. ↑ Walther DJ, Peter JU, Winter S, Holtje M, Paulmann N, Grohmann M, Vowinckel J, Alamo-Bethencourt V, Wilhelm CS, Ahnert-Hilger G, Bader M. Serotonylation of small GTPases is a signal transduction pathway that triggers platelet alpha-granule release. Cell. 2003 Dec 26;115(7):851-62. doi: 10.1016/s0092-8674(03)01014-6. PMID:14697203 doi:http://dx.doi.org/10.1016/s0092-8674(03)01014-6
3. ↑ Wallace SW, Magalhaes A, Hall A. The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells. Mol Cell Biol. 2011 Jan;31(1):81-91. doi: 10.1128/MCB.01001-10. Epub 2010 Oct 25. PMID:20974804 doi:10.1128/MCB.01001-10
4. ↑ Cachero TG, Morielli AD, Peralta EG. The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell. 1998 Jun 12;93(6):1077-85. doi: 10.1016/s0092-8674(00)81212-x. PMID:9635436 doi:http://dx.doi.org/10.1016/s0092-8674(00)81212-x
5. ↑ Tnimov Z, Guo Z, Gambin Y, Nguyen UT, Wu YW, Abankwa D, Stigter A, Collins BM, Waldmann H, Goody RS, Alexandrov K. Quantitative Analysis of Prenylated RhoA Interaction with Its Chaperone, RhoGDI. J Biol Chem. 2012 Aug 3;287(32):26549-62. Epub 2012 May 24. PMID:22628549 doi:10.1074/jbc.M112.371294