Journal
JOURNAL OF CELL BIOLOGY
Volume 178, Issue 1, Pages 155-165Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200612084
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Funding
- NCI NIH HHS [R01 CA095287, R01 CA95287] Funding Source: Medline
- NIAID NIH HHS [R01 AI35603, R01 AI53585, R01 AI055741, R01 AI053585, R01 AI035603, R01 AI55741] Funding Source: Medline
- NICHD NIH HHS [R01 HD25938, P01 HD025938] Funding Source: Medline
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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 Thr(2256), resulting in enhanced cell motility. Extracellular signal-regulated kinase phosphorylates NG2 at Thr(2314), stimulating cell proliferation. The effects of NG2 phosphorylation on proliferation and motility are dependent on beta 1-integrin activation. Differential cell surface localization of the two distinctly phosphorylated forms of NG2 may be the mechanism by which the l beta 1-integrin interaction promotes proliferation in one case and motility in the other. NG2 phosphorylated at Thr(2314) colocalizes with beta 1-integrin on microprotrusions from the apical cell surface. In contrast, NG2 phosphorylated at Thr(2256) colocalizes with beta 1-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.
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