Catch Muscle Myorod Modulates ATPase Activity of Myosin in a Phosphorylation-Dependent Way

被引：1

作者：

Matusovsky, Oleg S. ^{[1
,2
]}

Shevchenko, Ulyana V. ^{[1
]}

Matusovskaya, Galina G. ^{[1
]}

Sobieszek, Apolinary ^{[3
]}

Dobrzhanskaya, Anna V. ^{[1
]}

Shelud'ko, Nikolay S. ^{[1
]}

机构：

[1] Russian Acad Sci, Far East Branch, AV Zhirmunsky Inst Marine Biol, Vladivostok 690022, Russia

[2] Far Eastern Fed Univ, Sch Biomed, Vladivostok, Russia

[3] Austrian Acad Sci, Inst Biomed Aging Res, Innsbruck, Austria

来源：

PLOS ONE | 2015年 / 10卷 / 04期

基金：

俄罗斯科学基金会;

关键词：

THICK-FILAMENT PROTEIN; MOLLUSCAN MUSCLES; SMOOTH MUSCLES; TWITCHIN; ACTIN; PARAMYOSIN; INTERACTS; MECHANISM; STATE; ROD;

D O I：

10.1371/journal.pone.0125379

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 themyosin 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.

引用

页数：11