Myosin light chain phosphorylation does not modulate cross-bridge cycling rate in mouse skeletal muscle

Document Type

Article

Publication Date

1983

Abstract

An attempt was made to determine whether phosphorylation of the myosin light chain represents a thick filament-associated mechanism for modulating the rate of cross-bridge cycling in mouse skeletal muscle. When the degree of light chain phosphorylation was varied independently of tetanus duration, there was no correlation of phosphorylation with cross-bridge turnover rate, as measured by the shortening velocity of the muscle. It is concluded that in intact skeletal muscle phosphorylation of the myosin light chain does not in itself modulate cross-bridge cycling rate and that previously reported changes in cycling rate were due to other factors that may vary with tetanus duration.

Publication Title

Science

Volume

220

Issue

4602

First Page

1167

Last Page

1169

Comments

This article was published in Science, Volume 220, Issue 4602, Pages 1167-1169.

The published version is available at http://dx.doi.org/10.1126/science.6857239 .

Copyright © 1983 AAAS.

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