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A more recent version of this article appeared on March 1, 2006
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Submitted on July 5, 2005
Revised on December 5, 2005
Accepted on December 27, 2005
Regulates Myosin IIB Phosphorylation, Cellular Localization, and Filament Assembly
Department of Biochemistry, Institute of Medical Sciences, Faculty of Medicine, The Hebrew University, Jerusalem 91120, Israel
Monitoring Editor: Anne Ridley
Nonmuscle myosin II is an important component of the cytoskeleton, playing a major role in cell motility and chemotaxis. We have previously demonstrated that, on stimulation with epidermal growth factor (EGF), nonmuscle heavy chain myosin II-B (NMHC-IIB) undergoes a transient phosphorylation correlating with its cellular localization. We also showed that members of the PKC family are involved in this phosphorylation. Here we demonstrate that of the two conventional PKC isoforms expressed by prostate cancer cells, PKC 
II and PKC
, PKC directly phosphorylates NMHC-IIB. Overexpression of wild-type and kinase dead dominant negative PKC result in both altered NMHC-IIB phosphorylation and subcellular localization. We have also mapped the phosphorylation sites of PKC on NMHC-IIB. Conversion of the PKC phosphorylation sites to alanine residues, reduces the EGF-dependent NMHC-IIB phosphorylation. Aspartate substitution of these sites reduces NMHC-IIB localization into cytoskeleton. These results indicate that PKC regulates NMHC-IIB phosphorylation and cellular localization in response to EGF stimulation.
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