rhoB proto-oncogene protein; Rho-related GTP-binding protein RhoB; rho protein H6 (RHOB, ARH6, ARHB)
Jump to navigation
Jump to search
Function
- implicated in the assembly of focal adhesions & actin stress fibers
- mediates apoptosis in neoplastically transformed cells after DNA damage
- not essential for development but affects cell adhesion & growth factor signaling in transformed cells
- plays a negative role in tumorigenesis as deletion causes tumor formation
- involved in intracellular protein trafficking of a number of proteins
- targets PKN1 to endosomes & is involved in trafficking of the EGF receptor from late endosomes to lysosomes
- also required for stability & nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development
- binds ROCK1 & ROCK2
- also binds PKN1/PRK1
- interacts with ARGGEF3, RTKN & AKAP13
Structure
- belongs to the small GTPase superfamily, Rho family
Compartment
- prenylation specifies the subcellular location of RHOB
- farnesylated form is localized to the plasma membrane
- geranylgeranylated form is localized to the endosome
- late endosome membrane; lipid-anchor
- cell membrane; lipid-anchor
- nucleus
- also detected at the nuclear margin & in the nucleus
Pharmacology
- RHOB is a target of farnesyltransferase inhibitors, currently under investigation as antineoplastic agents
- farnesyltransferase inhibitor elevate levels of geranylgeranylated RHOB & cause mislocalization, leading to apoptosis & antineoplastic effects
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P62745.html
- ↑ Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/RHOBID42108ch2p24.html
- ↑ OMIM https://mirror.omim.org/entry/165380
- ↑ Kahn RA, Der CJ, Bokoch GM. The ras superfamily of GTP-binding proteins: guidelines on nomenclature. FASEB J. 1992 May;6(8):2512-3. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1592203
- ↑ Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature. 1994 Jan 6;367(6458):40-6. PMID: https://www.ncbi.nlm.nih.gov/pubmed/8107774
- ↑ Entrez Gene http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=388