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Myosin phosphatase target subunit 1 (MYPT1) regulates the contraction and relaxation of vascular smooth muscle and maintains blood pressure.
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Myosin phosphatase target subunit 1 (MYPT1) regulates the contraction and relaxation of vascular smooth muscle and maintains blood pressure.

Author: YN Qiao Affiliation: From the Key Laboratory of MOE for Modern Teaching Technology, Shaanxi Normal University, Xi'an 710062, China, Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.WQ He Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.CP Chen Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.CH Zhang Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.W Zhao Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.All authors
Edition/Format: Article Article : English
Publication:The Journal of biological chemistry, 2014 Aug 08; 289(32): 22512-23
Summary:
Myosin light chain phosphatase with its regulatory subunit, myosin phosphatase target subunit 1 (MYPT1) modulates Ca(2+)-dependent phosphorylation of myosin light chain by myosin light chain kinase, which is essential for smooth muscle contraction. The role of MYPT1 in vascular smooth muscle was investigated in adult MYPT1 smooth muscle specific knock-out mice. MYPT1 deletion enhanced phosphorylation of myosin  Read more...
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Document Type: Article
All Authors / Contributors: YN Qiao Affiliation: From the Key Laboratory of MOE for Modern Teaching Technology, Shaanxi Normal University, Xi'an 710062, China, Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; WQ He Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; CP Chen Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; CH Zhang Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; W Zhao Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; P Wang Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; L Zhang Affiliation: Zhejiang Provincial Key Laboratory for Technology and Application of Model Organisms, School of Life Sciences, Wenzhou Medical College, Wenzhou 325035, China.; YZ Wu Affiliation: From the Key Laboratory of MOE for Modern Teaching Technology, Shaanxi Normal University, Xi'an 710062, China.; X Yang Affiliation: State Key Laboratory of Proteomics, Genetic Laboratory of Development and Disease, Institute of Biotechnology, Beijing 100071, China, and.; YJ Peng Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China.; JM Gao Affiliation: Zhejiang Provincial Key Laboratory for Technology and Application of Model Organisms, School of Life Sciences, Wenzhou Medical College, Wenzhou 325035, China.; KE Kamm Affiliation: the Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9040.; JT Stull Affiliation: the Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9040.; MS Zhu Affiliation: Model Animal Research Center and MOE Key Laboratory of Animal Models of Disease, Nanjing University, Nanjing 210061, China, Zhejiang Provincial Key Laboratory for Technology and Application of Model Organisms, School of Life Sciences, Wenzhou Medical College, Wenzhou 325035, China, zhums@nju.edu.cn.
ISSN:0021-9258
Language Note: English
Unique Identifier: 5613395568
Awards:

Abstract:

Myosin light chain phosphatase with its regulatory subunit, myosin phosphatase target subunit 1 (MYPT1) modulates Ca(2+)-dependent phosphorylation of myosin light chain by myosin light chain kinase, which is essential for smooth muscle contraction. The role of MYPT1 in vascular smooth muscle was investigated in adult MYPT1 smooth muscle specific knock-out mice. MYPT1 deletion enhanced phosphorylation of myosin regulatory light chain and contractile force in isolated mesenteric arteries treated with KCl and various vascular agonists. The contractile responses of arteries from knock-out mice to norepinephrine were inhibited by Rho-associated kinase (ROCK) and protein kinase C inhibitors and were associated with inhibition of phosphorylation of the myosin light chain phosphatase inhibitor CPI-17. Additionally, stimulation of the NO/cGMP/protein kinase G (PKG) signaling pathway still resulted in relaxation of MYPT1-deficient mesenteric arteries, indicating phosphorylation of MYPT1 by PKG is not a major contributor to the relaxation response. Thus, MYPT1 enhances myosin light chain phosphatase activity sufficient for blood pressure maintenance. Rho-associated kinase phosphorylation of CPI-17 plays a significant role in enhancing vascular contractile responses, whereas phosphorylation of MYPT1 in the NO/cGMP/PKG signaling module is not necessary for relaxation.

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