Institut für Biomedizinische Alternsforschung


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Biochim. Biophys. Acta  2010;1804   
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Verlag der Österreichischen Akademie der Wissenschaften
Austrian Academy of Sciences Press
A-1011 Wien, Dr. Ignaz Seipel-Platz 2,
Tel. +43-1-515 81/DW 3420, Fax +43-1-515 81/DW 3400
https://verlag.oeaw.ac.at, e-mail: bestellung.verlag@oeaw.ac.at
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doi:10.1016/j.bbapap.2009.12.020


Thema: 11/ibapublikationen
Institut für Biomedizinische Alternsforschung


IBA Publikation









IBA Publikation





Biochim. Biophys. Acta  2010;1804   
Open access


Oleg S. Matusovsky, Nikolay S. Shelud'ko, Tatyana V. Permyakova, Magdalena Zukowska, Apolinary Sobieszek
Digital Object Icon  Catch muscle of bivalve molluscs contains myosin- and twitchin-associated protein kinase phosphorylating myorod ()
S.  884 - 890
Open access
doi:10.1016/j.bbapap.2009.12.020
Abstract:
We have shown previously that myorod, a molluscan thick filament protein of unknown function, is phosphorylated by vertebrate smooth myosin light chain kinase (MLCK) in N-terminal unique region. The aim of the present study was to clarify whether such phosphorylation may occur in molluscan muscles. We detected three kinases endogenous to molluscan catch muscle, namely, to the complex of surface thick filament proteins that consists of twitchin, myosin, and myorod. The first kinase was a protein kinase A because it was inhibited by a specific inhibitor; the second one was associated with twitchin and phosphorylated myorod at its N-terminal unique region independently of Ca2+; and the third kinase was bound to myosin and phosphorylated myorod as well as myosin in the C-terminal part of both proteins. The myosin-associated kinase was inhibited by micromolar concentration of calcium ions. This enzyme could be separated from myosin by chromatography, whereas the kinase associated with twitchin could not be separated from twitchin. Since twitchin has a MLCK-like domain, it is possible that this domain was responsible for myorod phosphorylation. Phosphorylation of myorod within the twitchin–myosin–myorod complex increased the actin-activated Mg2+-ATPase activity of myosin. Taken together, these results indicate that phosphorylation of myorod by kinases associated with key proteins of catch contraction may contribute to the functional activity of myorod in molluscan smooth muscle.

Keywords:  Molluscan-catch-muscle Myorod-phosphorylation Myosin Twitchin Twitchin-kinase
  2011/04/19 14:11:08
Document Date:  2010/01/13 15:08:00
Object Identifier:  0xc1aa5576 0x00273768
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Verlag der Österreichischen Akademie der Wissenschaften
Austrian Academy of Sciences Press
A-1011 Wien, Dr. Ignaz Seipel-Platz 2
Tel. +43-1-515 81/DW 3420, Fax +43-1-515 81/DW 3400
https://verlag.oeaw.ac.at, e-mail: verlag@oeaw.ac.at