Phosphorylation of NG2 proteoglycan by protein kinase C-α regulates polarized membrane distribution and cell motility

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

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)

Abstract

Protein Kinase C (PKC)-α 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 α3β1 integrin in apical cell surface protrusions. Phorbol ester treatment causes redistribution 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-α-mediated NG2 phosphorylation at Thr2256 is therefore a key step for initiating cell polarization and motility.

Original languageEnglish
Pages (from-to)55262-55270
Number of pages9
JournalJournal of Biological Chemistry
Volume279
Issue number53
DOIs
Publication statusPublished - Dec 31 2004

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Phosphorylation of NG2 proteoglycan by protein kinase C-α regulates polarized membrane distribution and cell motility'. Together they form a unique fingerprint.

Cite this