The effect of myosin light chain phosphorylation on the actin‐stimulated ATPase activity of myosin minifilaments

FEBS Letters

Levitsky, Dmitri I.²  Shuvalova, Lyudmila A.¹  Poglazov, Boris F.¹ 

[1] A.N. Bach Institute of Biochemistry of the Academy of Sciences of the USSR, Moscow 117071, USSR;A. N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow 119899, USSR

关键词: Myosin;    Phosphorylation;    Actin-myosin interaction;    ATP hydrolysis;    (Rabbit skeletal muscle);    LC2;    myosin light chain 2;   

DOI  :  10.1016/0014-5793(87)80355-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has been shown that in the absence of KCl, the actin-stimulated Mg²⁺-ATPase activity of rabbit skeletal myosin minifilaments with phosphorylated regulatory lights chains (LC₂) exceeds 3–4-fold that of myosin minifilaments with dephosphorylated LC₂. Addition of KCl leads to a decrease in the difference between the two ATPase activities. LC₂ phosphorylation considerably increases the rate of ATPase reaction and only slightly decreases the affinity of myosin minifilaments for F-actin. It is suggested that the unusual effect of LC₂ phosphorylation on the kinetic parameters of the actin-stimulated ATPase reaction of myosin minifilaments can be accounted for by its influence on the interaction between myosin heads which results in the ordered self-assembly of minifilaments.

【 授权许可】

Unknown