Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes

被引:30
作者
Bultot, Laurent [1 ]
Horman, Sandrine [1 ,2 ]
Neumann, Dietbert [3 ]
Walsh, Michael P. [4 ,5 ]
Hue, Louis [1 ]
Rider, Mark H. [1 ]
机构
[1] Univ Catholique Louvain, Hormone & Metab Res Unit, de Duve Inst, B-1200 Brussels, Belgium
[2] Univ Catholique Louvain, CARD Unit, Div Cardiol, B-1200 Brussels, Belgium
[3] ETH, Swiss Fed Inst Technol, Inst Cell Biol, CH-8093 Zurich, Switzerland
[4] Univ Calgary, Smooth Muscle Res Grp, Fac Med, Calgary, AB T2N 4N1, Canada
[5] Univ Calgary, Dept Biochem & Mol Biol, Fac Med, Calgary, AB T2N 4N1, Canada
基金
英国医学研究理事会;
关键词
AMPK; Myosin light chain; Phosphorylation; Energy deprivation; Cell structure; ACTIVATED PROTEIN-KINASE; SMOOTH-MUSCLE MYOSIN; PHOSPHORYLATION; CONTRACTION; PURIFICATION; ISCHEMIA; POLARITY; LKB1;
D O I
10.1016/j.febslet.2008.11.022
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 kinetics of myosin regulatory light chain (MLC) phosphorylation by recombinant AMP-activated protein kinase (AMPK) were compared with commercial AMPK from rat liver and smooth muscle myosin light chain kinase (smMLCK). With identical amounts of activity units, initial rates of phosphorylation of MLC were at least 100-fold less with recombinant AMPK compared to smMLCK, whereas with rat liver AMPK significant phosphorylation was seen. In Madin-Darby Canine Kidney cells, AMPK activation led to an increase in MLC phosphorylation, which was decreased by a Rho kinase inhibitor without affecting AMPK activation. Therefore, MLC phosphorylation during energy deprivation does not result from direct phosphorylation by AMPK.
引用
收藏
页码:25 / 28
页数:4
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