Regulation by molluscan myosins

Molluscan myosins are regulated molecules that control muscle contraction by the selective binding of calcium. The essential and the regulatory light chains are regulatory subunits. Scallop myosin is the favorite material for studying the interactions of the light chains with the myosin heavy chain...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1999-01, Vol.190 (1-2), p.55-62
Main Authors: Szent-Györgyi, A G, Kalabokis, V N, Perreault-Micale, C L
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
Animals
Calcium
Light
Marine
Molecular Sequence Data
Mollusca
Mollusca - chemistry
Mollusks
Muscles
Myosin-Light-Chain Kinase - metabolism
Myosins - chemistry
Myosins - metabolism
Myosins - physiology
Phosphorylation
Proteins
Regulation
Sequence Homology, Amino Acid
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Summary:Molluscan myosins are regulated molecules that control muscle contraction by the selective binding of calcium. The essential and the regulatory light chains are regulatory subunits. Scallop myosin is the favorite material for studying the interactions of the light chains with the myosin heavy chain since the regulatory light chains can be reversibly removed from it and its essential light chains can be exchanged. Mutational and structural studies show that the essential light chain binds calcium provided that the Ca-binding loop is stabilized by specific interactions with the regulatory light chain and the heavy chain. The regulatory light chains are inhibitory subunits. Regulation requires the presence of both myosin heads and an intact headrod junction. Heavy meromyosin is regulated and shows cooperative features of activation while subfragment-1 is non-cooperative. The myosin heavy chains of the functionally different phasic striated and the smooth catch muscle myosins are products of a single gene, the isoforms arise from alternative splicing. The differences between residues of the isoforms are clustered at surface loop-1 of the heavy chain and account for the different ATPase activity of the two muscle types. Catch muscles contain two regulatory light chain isoforms, one phosphorylatable by gizzard myosin light chain kinase. Phosphorylation of the light chain does not alter ATPase activity. We could not find evidence that light chain phosphorylation is responsible for the catch state.
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1006975705724