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Myosin S2 is not required for effects of myosin binding protein‐C on motility
Author(s) -
Shaffer Justin F.,
Razumova Maria V.,
Tu An-Yue,
Regnier Michael,
Harris Samantha P.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.007
Subject(s) - myosin , motility , heavy meromyosin , actin , meromyosin , biology , myosin light chain kinase , microbiology and biotechnology , myosin head , biochemistry , biophysics
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.