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Article

Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain.

The Journal of cell biology - 1 Mar 1994

Trybus K M, Waller G S, Chatman T A

Abstract excerpt

Smooth muscle myosin acts as a molecular motor only if the regulatory light chain (RLC) is phosphorylated. This subunit can be removed from myosin by a novel method involving the use of trifluoperazine. The motility of RLC-deficient myosin is very slow, but native properties are restored when RLC is rebound. Truncating 6 residues from the COOH terminus of the RLC had no effect on phosphorylated myosin's motor...

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Identifiers

PMID: 8132717
DOI: 10.1083/jcb.124.6.963
PMCID: PMC2119978

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain.PMID 8132717Read ↗

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