作者
Cai‐Ping Chen, Xin Chen, Yan‐Ning Qiao, Pei Wang, Wei‐Qi He, Cheng‐Hai Zhang, Wei Zhao, Yun‐Qian Gao, Chen Chen, Tao Tao, Jie Sun, Ye Wang, Ning Gao, Kristine E Kamm, James T Stull, Min‐Sheng Zhu
发表日期
2015/2/1
期刊
The Journal of physiology
卷号
593
期号
3
页码范围
681-700
简介
Key points
- Force production and maintenance in smooth muscle is largely controlled by myosin regulatory light chain (RLC) phosphorylation, which relies on a balance between Ca2+/calmodulin‐dependent myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) activities.
- MYPT1 is the regulatory subunit of MLCP that biochemically inhibits MLCP activity via T694 or T852 phosphorylation in vitro.
- Here we separately investigated the contribution of these two phosphorylation sites in bladder smooth muscles by establishing two single point mutation mouse lines, T694A and T852A, and found that phosphorylation of MYPT1 T694, but not T852, mediates force maintenance via inhibition of MLCP activity and enhancement of RLC phosphorylation in vivo.
- Our findings reveal the role of MYPT1 T694/T852 phosphorylation in vivo in regulation of smooth muscle contraction.
Abstract
Force …
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CP Chen, X Chen, YN Qiao, P Wang, WQ He… - The Journal of physiology, 2015