Pseudo-phosphorylation of essential light chains affects the functioning of skeletal muscle myosin

被引：0
|
作者：
Yampolskaya, Daria S. [1 ]
V. Kopylova, Galina [2 ]
Shchepkin, Daniil, V [2 ]
Nabiev, Salavat R. [2 ]
V. Nikitina, Larisa [2 ]
Walklate, Jonathan [3 ]
Ziganshin, Rustam H. [4 ]
Bershitsky, Sergey Y. [2 ]
Geeves, Michael A. [3 ]
Matyushenko, Alexander M. [1 ]
Levitsky, Dmitrii I. [1 ]
机构：
[1] Russian Acad Sci, Bach Inst Biochem, Res Ctr Biotechnol, Leninsky prosp 33, Moscow 119071, Russia
[2] Russian Acad Sci, Inst Immunol & Physiol, Ekaterinburg 620049, Russia
[3] Univ Kent, Sch Biosci, Canterbury CT2 7NJ, Kent, England
[4] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Ul Miklukho-Maklaya 16-10, Moscow 117997, Russia
来源：
BIOPHYSICAL CHEMISTRY | 2023年 / 292卷
关键词：
Myosin; Essential light chain; Pseudo-phosphorylation; Actin-myosin interaction; Mechanism of muscle contraction; MOTOR DOMAIN; STABILIZING SUBSTITUTIONS; MOLECULAR-MECHANISMS; SHORTENING VELOCITY; CARDIAC MYOSIN; ATP TURNOVER; ADP RELEASE; ACTIN; HEAD; SUBFRAGMENT-1;
D O I：
10.1016/j.bpc.2022.106936
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The work aimed to investigate how the phosphorylation of the myosin essential light chain of fast skeletal myosin (LC1) affects the functional properties of the myosin molecule. Using mass-spectrometry, we revealed phos-phorylated peptides of LC1 in myosin from different fast skeletal muscles. Mutations S193D and T65D that mimic natural phosphorylation of LC1 were produced, and their effects on functional properties of the entire myosin molecule and isolated myosin head (S1) were studied. We have shown that T65D mutation drastically decreased the sliding velocity of thin filaments in an in vitro motility assay and strongly increased the duration of actin-myosin interaction in optical trap experiments. These effects of T65D mutation in LC1 observed only with the whole myosin but not with S1 were prevented by double T65D/S193D mutation. The T65D and T65D/S193D mutations increased actin-activated ATPase activity of S1 and decreased ADP affinity for the actin-S1 complex. The results indicate that pseudo-phosphorylation of LC1 differently affects the properties of the whole myosin molecule and its isolated head. Also, the results show that phosphorylation of LC1 of skeletal myosin could be one more mechanism of regulation of actin-myosin interaction that needs further investigation.
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页数：9
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