Article
Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility.
The Journal of biological chemistry - 31 Dec 2004
Makagiansar Irwan T, Williams Scott, Dahlin-Huppe Kimberlee, Fukushi Jun-ichi, Mustelin Tomas, Stallcup William B
Abstract excerpt
Protein kinase C (PKC)-alpha phosphorylation of recombinant NG2 cytoplasmic domain and phorbol ester-induced PKC-dependent phosphorylation of full-length NG2 expressed in U251 cells are both blocked by mutation of Thr(2256), identifying this residue as a primary phosphorylation site. In untreated U251/NG2 cells, NG2 is present along with ezrin and alpha(3)beta(1) integrin in apical cell surface protrusions....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.