Regulation of contraction by calcium binding myosins
References (29)
- et al.
Biochim. Biophys. Acta
(1959) - et al.
J. Mol. Biol.
(1971) - et al.
J. Mol. Biol.
(1970) - et al.
J. Mol. Biol.
(1973) - et al.
J. Mol. Biol.
(1980) - et al.
J. Mol. Biol.
(1980) - et al.
Biochimie
(1981) - et al.
J. Biol. Chem.
(1991) - et al.
- et al.
J. Muscle Res. Cell Motil.
(1981)
Science
Nature (London)
J. Physiol.
Cited by (24)
Crystal structure of a phosphorylated light chain domain of scallop smooth-muscle myosin
2011, Biophysical JournalCitation Excerpt :Regulation of molluscan muscle myosins is controlled by direct binding of Ca2+ to the essential light chain (ELC) (2). Calcium binding to the ELC mediates the communication between the ELC and the regulatory light chain (RLC), such that regulation in molluscan myosin requires both light chains (3). To investigate regulation in molluscan myosin, our laboratory previously determined the crystal structures of Ca2+-bound and Ca2+-free scallop striated muscle light chain domains (LCDs) (4,5).
Spectroscopic and ITC study of the conformational change upon Ca<sup>2+</sup>-binding in TnC C-lobe and TnI peptide complex from Akazara scallop striated muscle
2008, Biochemical and Biophysical Research CommunicationsAn Unstable Head-Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated Myosins
2008, Journal of Molecular BiologyMyosin cross-bridge kinetics and the mechanism of catch
2007, Biophysical JournalCitation Excerpt :When twitchin is unphosphorylated, catch force is maintained; and when twitchin is phosphorylated, catch force is relaxed. Activation of myosin cross-bridge cycling in molluscan catch muscles results from calcium binding to myosin (for review, see (6,7)), and at every subsaturating [Ca+2], there is a catch component of force output which is relaxed by phosphorylation of twitchin (5). The mechanism of catch force maintenance is not known.