Regulation of angiogenesis is often viewed as a balance between pro-angiogenic and anti-angiogenic factors, and when the balance shifts in favour of angiogenesis stimulators, an angiogenic switch turns on the normally inactive endothelial cells to grow new blood vessels. Recent studies have shown that PLCγ1 (phospholipase Cγ1), a major signalling substrate of VEGFR-2 (vascular endothelial growth factor receptor 2), undergoes c-Cbl-mediated ubiquitination. c-Cbl suppresses tyrosine phosphorylation of PLCγ1 and with it VEGF (vascular endothelial growth factor)-induced endothelial cell proliferation and angiogenesis. Loss of c-Cbl in mice results in enhanced retinal neovascularization, VEGF- and tumour-induced angiogenesis. Notably, this observation suggests that c-Cbl-mediated ubiquitination pathway plays a central role in the ‘angiogenic switch’ employed by the VEGF system. The present article highlights the recent findings demonstrating a novel role for protein ubiquitination in angiogenesis and its potential in angiogenesis-based therapy.
Skip Nav Destination
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article| November 19 2009
A role for protein ubiquitination in VEGFR-2 signalling and angiogenesis
Nader Rahimi 1
1Departments of Pathology and Ophthalmology, Boston University School of Medicine, 670 Albany Street, Boston, MA 02118, U.S.A.
Search for other works by this author on:
Biochem Soc Trans (2009) 37 (6): 1189–1192.
June 26 2009
Nader Rahimi; A role for protein ubiquitination in VEGFR-2 signalling and angiogenesis. Biochem Soc Trans 1 December 2009; 37 (6): 1189–1192. doi: https://doi.org/10.1042/BST0371189
Download citation file:
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your InstitutionSign in via your Institution
Get Access To This Article
Buy This Article