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J Muscle Res Cell Motil. 2001;22(2):163-73.

Regulation of nonmuscle myosins by heavy chain phosphorylation.

Author information

1
Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland. jolanta@nencki.gov.pl

Abstract

Functional activities of many nonmuscle myosin isoforms are (or are postulated to be) regulated by heavy chain phosphorylation. Depending on the myosin isoform, the serine or threonine residues located within the head (myosin I or myosin VI) or within the C-terminal tail domains (myosin II or myosin V) can be phosphorylated by more or less specific endogenous kinases. In some isoforms phosphorylation can occur both in the head and tail domains, as it has been found for myosin III. There are also isoforms that can be regulated both by the heavy and regulatory light chain phosphorylation, as for the example myosin II from slide mold Dictyostelium discoideum. The goal of this review was to describe recent findings on regulation of myosin I, myosin II, myosin III, myosin V and myosin VI isoforms by their heavy chain phosphorylation including the short charcteristics of the relevant kinases. The biological aspects of the phosphorylation are also discussed.

PMID:
11519739
[Indexed for MEDLINE]

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