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Published online June 25, 2007
doi:10.1083/jcb.200612084
The Journal of Cell Biology, Vol. 178, No. 1, 155-165
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Makagiansar et al.
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Article

 Differential phosphorylation of NG2 proteoglycan by ERK and PKC{alpha} helps balance cell proliferation and migration

Irwan T. Makagiansar, Scott Williams, Tomas Mustelin, and William B. Stallcup

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

Correspondence to Irwan T. Makagiansar: irwan.makagiansar{at}emdbiosciences.com

Two distinct Thr phosphorylation events within the cytoplasmic domain of the NG2 proteoglycan help regulate the cellular balance between proliferation and motility. Protein kinase C{alpha} mediates the phosphorylation of NG2 at Thr2256, resulting in enhanced cell motility. Extracellular signal–regulated kinase phosphorylates NG2 at Thr2314, stimulating cell proliferation. The effects of NG2 phosphorylation on proliferation and motility are dependent on ß1-integrin activation. Differential cell surface localization of the two distinctly phosphorylated forms of NG2 may be the mechanism by which the NG2–ß1-integrin interaction promotes proliferation in one case and motility in the other. NG2 phosphorylated at Thr2314 colocalizes with ß1-integrin on microprotrusions from the apical cell surface. In contrast, NG2 phosphorylated at Thr2256 colocalizes with ß1-integrin on lamellipodia at the leading edges of cells. Thus, phosphorylation and the resulting site of NG2–integrin localization may determine the specific downstream effects of integrin signaling.

I.T. Makagiansar's present address is EMD Biosciences, Inc., San Diego, CA 92121.

S. Williams' present address is Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121.

T. Mustelin's present address is Amgen, Inc., Seattle, WA 98119.

Abbreviations used in this paper: ERK, extracellular signal–regulated kinase; FAK, focal adhesion kinase; MEK, MAPK kinase; P-ERK, phosphorylated ERK.


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