Myosin light chain kinase colocalizes with nonmuscle myosin IIB in myofibril precursors and sarcomeric Z-lines of cardiomyocytes

Cell Motility and the Cytoskeleton
T V DudnakovaV P Shirinsky

Abstract

Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility involving actin and myosin II. MLCK is widely present in vertebrate tissues including the myocardium. However, the role of MLCK in cardiomyocyte function is not known. Previous attempts to gain insight into possible roles and identify potential molecular partners were disappointing and equivocal due to cross reactivity of early antibodies with striated muscle MLCK, which has a different genetic locus and a divergent amino acid sequence from the above mentioned enzyme. Using an immunofluorescence approach and a panel of antibodies directed against MLCK, cytoskeletal, and sarcomeric proteins, we localized MLCK to myofibril precursors and Z-lines of sarcomeres in embryonic and adult cardiomyocytes. The same structures contained nonmuscle myosin IIB implicating this protein as a possible target of MLCK. Our results suggest a role for MLCK in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin IIB.

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Oct 28, 2003·Molecular and Cellular Biochemistry·Tatyana V DudnakovaValeri I Kapelko
Jul 22, 2004·Experimental Cell Research·Dmitry S KudryashovVladimir P Shirinsky
Apr 6, 2005·Cell Motility and the Cytoskeleton·Jushuo WangJoseph W Sanger

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Citations

May 14, 2008·The Journal of Biological Chemistry·Jian HuangJames T Stull
Nov 29, 2011·Biochemical and Biophysical Research Communications·Matthew P JosephsonKatalin Ajtai
Dec 10, 2009·Journal of Muscle Research and Cell Motility·Anthony J KeeEdna C Hardeman

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