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Papers In Press, published online ahead of print October 25, 2004
J. Biol. Chem, 10.1074/jbc.M411045200
Submitted on September 27, 2004
Revised on October 25, 2004
Accepted on October 25, 2004

Phosphorylation of NG2 proteoglycan by PKC-alpha regulates polarized membrane distribution and cell motility

Irwan T. Makagiansar, Scott Williams, Kimberlee Dahlin-Huppe, Jun-ichi Fukushi, Tomas Mustelin, and William B. Stallcup

Cancer Research Center, The Burnham Institute, La Jolla, CA 92037

Corresponding Author: irwanm{at}burnham.org

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 T2256, identifying this residue as a primary phosphorylation site. In untreated U251/NG2 cells, NG2 is present along with ezrin and alpha 3beta 1 integrin in apical cell surface protrusions. Phorbol ester treatment causes re-distribution of all three components to lamellipodia, accompanied by increased cell motility. U251 cells expressing NG2 with a valine substitution at position 2256 are resistant to phorbol ester treatment: NG2 remains in membrane protrusions and cell motility is unchanged. In contrast, NG2 with a glutamic acid substitution at position 2256 redistributes to lamellipodia even without phorbol ester treatment, rendering transfected U251 cells spontaneously motile. PKC-alpha -mediated NG2 phosphorylation at T2256 is therefore a key step for initiating cell polarization and motility.


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