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Cell Motil Cytoskeleton. 1991;18(2):81-5.

Regulation of smooth muscle myosin.

Author information

1
Rosenstiel Research Center, Brandeis University, Waltham, MA 02254.

Abstract

It is well established that light chain phosphorylation is required before a smooth muscle can generate force. The apparent modulation of shortening velocity by phosphorylation during sustained contractions may be accounted for by a mechanical interaction between rapidly cycling phosphorylated crossbridges and slowly or non-cycling dephosphorylated crossbridges. Latchbridges, force-producing dephosphorylated crossbridges, have been proposed to explain why force levels remain high at low levels of phosphorylation. The role of the thin-filament-associated proteins caldesmon and calponin in regulation remains enigmatic, but their inhibitory properties in solution would be consistent with a possible involvement in maintenance of a relaxed state.

PMID:
1826467
DOI:
10.1002/cm.970180202
[Indexed for MEDLINE]

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