Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In the present study, MM-CK is found to physically interact with the slow skeletal muscle-type MyBPC1 (myosin-binding protein C1). The interaction between MyBPC1 and MM-CK depended on the creatine concentration in a dose-dependent manner, but not on ATP, ADP or phosphocreatine. The MyBPC1–CK interaction favoured acidic conditions, and the two molecules dissociated at above pH 7.5. Domain-mapping experiments indicated that MM-CK binds to the C-terminal domains of MyBPC1, which is also the binding site of myosin. The functional coupling of myosin, MyBPC1 and MM-CK is further corroborated using an ATPase activity assay in which ATP expenditure accelerates upon the association of the three proteins, and the apparent Km value of myosin is therefore reduced. The results of the present study suggest that MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (MM-CK) for efficient energy metabolism and homoeostasis.
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Research Article|
May 13 2011
Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin
Zhe Chen;
Zhe Chen
*State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China
†Protein Science Laboratory of the Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China
‡National Engineering Laboratory for Anti-Tumor Protein Therapeutics, School of Life Sciences, Tsinghua University, Beijing 100084, China
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Tong-Jin Zhao;
Tong-Jin Zhao
1
*State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China
†Protein Science Laboratory of the Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China
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Jie Li;
Jie Li
†Protein Science Laboratory of the Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China
‡National Engineering Laboratory for Anti-Tumor Protein Therapeutics, School of Life Sciences, Tsinghua University, Beijing 100084, China
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Yan-Song Gao;
Yan-Song Gao
1
*State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China
†Protein Science Laboratory of the Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China
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Fan-Guo Meng;
Fan-Guo Meng
§Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang 314006, China
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Yong-Bin Yan;
Yong-Bin Yan
2
*State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China
2Correspondence may be addressed to either of these authors (email ybyan@tsinghua.edu.cn or zhm-dbs@tsinghua.edu.cn).
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Hai-Meng Zhou
Hai-Meng Zhou
2
†Protein Science Laboratory of the Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China
‡National Engineering Laboratory for Anti-Tumor Protein Therapeutics, School of Life Sciences, Tsinghua University, Beijing 100084, China
§Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang 314006, China
2Correspondence may be addressed to either of these authors (email ybyan@tsinghua.edu.cn or zhm-dbs@tsinghua.edu.cn).
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Publisher: Portland Press Ltd
Received:
December 01 2010
Revision Received:
March 03 2011
Accepted:
March 22 2011
Accepted Manuscript online:
March 22 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 436 (2): 437–445.
Article history
Received:
December 01 2010
Revision Received:
March 03 2011
Accepted:
March 22 2011
Accepted Manuscript online:
March 22 2011
Citation
Zhe Chen, Tong-Jin Zhao, Jie Li, Yan-Song Gao, Fan-Guo Meng, Yong-Bin Yan, Hai-Meng Zhou; Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin. Biochem J 1 June 2011; 436 (2): 437–445. doi: https://doi.org/10.1042/BJ20102007
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