REGULATION OF CALMODULIN-BINDING MYOSINS

Authors
Citation
Js. Wolenski, REGULATION OF CALMODULIN-BINDING MYOSINS, Trends in cell biology, 5(8), 1995, pp. 310-316
Citations number
58
Categorie Soggetti
Cell Biology
Journal title
ISSN journal
09628924
Volume
5
Issue
8
Year of publication
1995
Pages
310 - 316
Database
ISI
SICI code
0962-8924(1995)5:8<310:ROCM>2.0.ZU;2-8
Abstract
Myosins constitute a diverse superfamily of actin-based mechanoenzymes that are involved in many essential cellular motilities. In addition to conventional muscle myosin II, ten other classes of unconventional myosins are known. Many unconventional myosins bind multiple calmoduli n light chains and Ca2+, which can dramatically alter their mechanoche mical and enzymatic activity. Calmodulin-binding myosins can also be r egulated by phospholipid binding, phosphorylation of the heavy chain a nd actin-binding proteins. The molecular details linking unconventiona l-myosin regulation and function are just beginning to emerge.