QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 17, Issue 3, 1364-1374, March 2006

This Article Full Text Full Text (PDF) All Versions of this Article: E05-07-0597v1 17/3/1364    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rosenberg, M. Articles by Ravid, S. Search for Related Content PubMed PubMed Citation Articles by Rosenberg, M. Articles by Ravid, S.

Protein Kinase C 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

Submitted July 5, 2005; Revised December 5, 2005; Accepted December 27, 2005
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 myosin heavy chain 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, PKCII 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.

Address correspondence to: Shoshana Ravid (ravid{at}cc.huji.ac.il).

This article has been cited by other articles:

				M. Parsons and J. C. Adams Rac regulates the interaction of fascin with protein kinase C in cell migration J. Cell Sci., September 1, 2008; 121(17): 2805 - 2813. [Abstract] [Full Text] [PDF]

				S. Komatsu and M. Ikebe The Phosphorylation of Myosin II at the Ser1 and Ser2 Is Critical for Normal Platelet-derived Growth Factor induced Reorganization of Myosin Filaments Mol. Biol. Cell, December 1, 2007; 18(12): 5081 - 5090. [Abstract] [Full Text] [PDF]

				N. G. Dulyaninova, R. P. House, V. Betapudi, and A. R. Bresnick Myosin-IIA Heavy-Chain Phosphorylation Regulates the Motility of MDA-MB-231 Carcinoma Cells Mol. Biol. Cell, August 1, 2007; 18(8): 3144 - 3155. [Abstract] [Full Text] [PDF]

				M. K. Sato, M. Takahashi, and M. Yazawa Two Regions of the Tail Are Necessary for the Isoform-specific Functions of Nonmuscle Myosin IIB Mol. Biol. Cell, March 1, 2007; 18(3): 1009 - 1017. [Abstract] [Full Text] [PDF]

				G. I. Gorodeski Estrogen Modulation of MgATPase Activity of Nonmuscle Myosin-II-B Filaments Endocrinology, January 1, 2007; 148(1): 279 - 292. [Abstract] [Full Text] [PDF]

				J. C. Sandquist, K. I. Swenson, K. A. DeMali, K. Burridge, and A. R. Means Rho Kinase Differentially Regulates Phosphorylation of Nonmuscle Myosin II Isoforms A and B during Cell Rounding and Migration J. Biol. Chem., November 24, 2006; 281(47): 35873 - 35883. [Abstract] [Full Text] [PDF]

				L. Even-Faitelson and S. Ravid PAK1 and aPKC{zeta} Regulate Myosin II-B Phosphorylation: A Novel Signaling Pathway Regulating Filament Assembly Mol. Biol. Cell, July 1, 2006; 17(7): 2869 - 2881. [Abstract] [Full Text] [PDF]