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Papers In Press, published online ahead of print November 6, 2000
Dept of Molecular Pathogenesis, Div Adult Diseases, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 101-0062
Corresponding Author: akitis{at}mri.tmd.ac.jp
Myosin light chain phosphatase consists of three subunits, a 38 kDa catalytic subunit, a large 110-130 kDa myosin binding subunit, and a small subunit of 20-21 kDa. The catalytic subunit and the large subunit have been well characterized. The small subunit has been cloned and studied from smooth muscle, but little is known about its function and specificity in the other muscles such as cardiac muscle. In this study, cDNAs for heart-specific small subunit isoforms, hHS-M21, were isolated and characterized. Evidence was obtained from an analysis of genome to suggest that the small subunit was the product of the same gene as the large subunit. Using permeabilized renal artery preparation and permeabilized cardiac myocytes, it was shown that the small subunit increased sensitivity to Ca2+ in muscle contraction. It was also shown using an overlay assay that hHS-M21 bound the large subunit. Mapping experiments demonstrated that the binding domain and the domain involved in the increasing Ca2+ sensitivity mapped to the same N-terminal region of hHS-M21. These observations suggest that the heart-specific small subunit hHS-M21 plays a regulatory role in cardiac muscle contraction by its binding to the large subunit.
J. Biol. Chem, 10.1074/jbc.M008566200
Submitted on September 19, 2000
Revised on November 3, 2000
Accepted on November 6, 2000
Identification, characterization and functional analysis of heart-specific myosin light chain phosphatase small subunit
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