Catch muscle myorod modulates ATPase activity of Myosin in a phosphorylation-dependent way

Myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of the myosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. The u...

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Bibliographic Details
Published in:PloS one 2015-04, Vol.10 (4), p.e0125379-e0125379
Main Authors: Matusovsky, Oleg S, Shevchenko, Ulyana V, Matusovskaya, Galina G, Sobieszek, Apolinary, Dobrzhanskaya, Anna V, Shelud'ko, Nikolay S
Format: Article
Language:English
Subjects:
Actin
Actomyosin - metabolism
Adenosine triphosphatase
Alternative splicing
Animals
Bivalvia
Bivalvia - metabolism
Bivalvia - physiology
Ca(2+) Mg(2+)-ATPase - metabolism
Chains
Chemical Precipitation
Chemical properties
Chromatography
Filaments
Gizzard
Kinases
Magnesium
Marine biology
Mollusca
Mollusks
Muscle Contraction - physiology
Muscle proteins
Muscle Proteins - isolation & purification
Muscle Proteins - metabolism
Muscle Proteins - physiology
Muscle, Smooth - enzymology
Muscle, Smooth - metabolism
Muscle, Smooth - physiology
Muscles
Myosin
Myosin-light-chain kinase
Myosins - metabolism
N-Terminus
Phosphorylation
Polymerization
Potentiation
Proteins
Smooth muscle
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Summary:Myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of the myosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. The unique domain is a target for phosphorylation by gizzard smooth myosin light chain kinase (smMLCK) and, perhaps, molluscan twitchin, which contains a MLCK-like domain. To elucidate the role of myorod and its phosphorylation in the catch muscle, the effect of chromatographically purified myorod on the actin-activated Mg2+-ATPase activity of myosin was studied. We found that phosphorylation at the N-terminus of myorod potentiated the actin-activated Mg2+-ATPase activity of mussel and rabbit myosins. This potentiation occurred only if myorod was phosphorylated and introduced into the ATPase assay as a co-filament with myosin. We suggest that myorod could be related to the catch state, a function specific to molluscan muscle.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0125379