Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin

Zhe Chen, Tong Jin Zhao, Jie Li, Yan Song Gao, Fan Guo Meng, Yong Bin Yan, Hai Meng Zhou

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


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, MMCK 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. TheMyBPC1-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.

Original languageEnglish (US)
Pages (from-to)437-445
Number of pages9
JournalBiochemical Journal
Issue number2
StatePublished - Jun 1 2011


  • ATPase activity
  • Energy homoeostasis
  • Muscle-type creatine kinase (MM-CK)
  • Myosin
  • Sarcomere
  • Slow skeletal muscle-type myosin-binding protein C (MYBPC)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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