RhoA Recombinant Rabbit Monoclonal Antibody [SN0612]

Function

Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the RHOA gene. While the effects of RhoA activity are not all well known, it is primarily associated with cytoskeleton regulation, mostly actin stress fibers formation and actomyosin contractility. It acts upon several effectors. Among them, ROCK1 (Rho-associated, coiled-coil containing protein kinase 1) and DIAPH1 (Diaphanous Homologue 1, a.k.a. hDia1, homologue to mDia1 in mouse, diaphanous in Drosophila) are the best described. RhoA, and the other Rho GTPases, are part of a larger family of related proteins known as the Ras superfamily, a family of proteins involved in the regulation and timing of cell division. RhoA is one of the oldest Rho GTPases, with homologues present in the genomes since 1.5 billion years. As a consequence, RhoA is somehow involved in many cellular processes which emerged throughout evolution. RhoA specifically is regarded as a prominent regulatory factor in other functions such as the regulation of cytoskeletal dynamics, transcription, cell cycle progression and cell transformation.

Background References

1. Freeman MC et al. Coronaviruses induce entry-independent, continuous macropinocytosis. MBio 5:e01340-14 (2014).

2. Nuno DW et al. RhoA localization with caveolin-1 regulates vascular contractions to serotonin. Am J Physiol Regul Integr Comp Physiol 303:R959-67 (2012).

Sequence Similarity

Belongs to the small GTPase superfamily. Rho family.

Post-translational Modification

(Microbial infection) Substrate for botulinum ADP-ribosyltransferase.; (Microbial infection) Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.; (Microbial infection) AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.; (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly.; Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling. Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).; Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons.

Subcellular Location

Cell membrane, Cytoplasm, Cleavage furrow, Midbody, Cell projection.

UNIPROT

SwissProt: P61586 Human

SwissProt: Q9QUI0 Mouse

SwissProt: P61589 Rat

Synonyms