Myosin S2 is not required for effects of myosin binding protein-C on motility

Justin F. Shaffer, Maria V. Razumova, An Yue Tu, Michael Regnier, Samantha P. Harris

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


The unique myosin binding protein-c "motif" near the N-terminus of myosin binding protein-C (MyBP-C) binds myosin S2. Previous studies demonstrated that recombinant proteins containing the motif and flanking regions (e.g., C1C2) affect thin filament movement in motility assays using heavy meromyosin (S1 plus S2) as the molecular motor. To determine if S2 is required for these effects we investigated whether C1C2 affects motility in assays using only myosin S1 as the motor protein. Results demonstrate that effects of C1C2 are comparable in both systems and suggest that the MyBP-C motif affects motility through direct interactions with actin and/or myosin S1.

Original languageEnglish (US)
Pages (from-to)1501-1504
Number of pages4
JournalFEBS Letters
Issue number7
StatePublished - Apr 3 2007


  • Motility
  • Muscle
  • Myosin
  • Myosin binding protein-C

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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