{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hessel AL"],"funding":["NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["2628"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10960836"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Muscle contraction is produced via the interaction of myofilaments and is regulated so that muscle performance matches demand. Myosin-binding protein C (MyBP-C) is a long and flexible protein that is tightly bound to the thick filament at its C-terminal end (MyBP-C<sup>C8C10</sup>), but may be loosely bound at its middle- and N-terminal end (MyBP-C<sup>C1C7</sup>) to myosin heads and/or the thin filament. MyBP-C is thought to control muscle contraction via the regulation of myosin motors, as mutations lead to debilitating disease. We use a combination of mechanics and small-angle X-ray diffraction to study the immediate and selective removal of the MyBP-C<sup>C1C7</sup> domains of fast MyBP-C in permeabilized skeletal muscle. We show that cleavage leads to alterations in crossbridge kinetics and passive structural signatures of myofilaments that are indicative of a shift of myosin heads towards the ON state, highlighting the importance of MyBP-C<sup>C1C7</sup> to myofilament force production and regulation."],"journal":["Nature communications"],"pubmed_title":["Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads."],"pmcid":["PMC10960836"],"funding_grant_id":["P30 GM138395","T32 HL007249","P41 GM103622"],"pubmed_authors":["Linke WA","Nissen D","Engels NM","Kuehn MN","Harris SP","Hessel AL","Sadler RL","Irving TC","Ma W"],"additional_accession":[]},"is_claimable":false,"name":"Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.","description":"Muscle contraction is produced via the interaction of myofilaments and is regulated so that muscle performance matches demand. Myosin-binding protein C (MyBP-C) is a long and flexible protein that is tightly bound to the thick filament at its C-terminal end (MyBP-C<sup>C8C10</sup>), but may be loosely bound at its middle- and N-terminal end (MyBP-C<sup>C1C7</sup>) to myosin heads and/or the thin filament. MyBP-C is thought to control muscle contraction via the regulation of myosin motors, as mutations lead to debilitating disease. We use a combination of mechanics and small-angle X-ray diffraction to study the immediate and selective removal of the MyBP-C<sup>C1C7</sup> domains of fast MyBP-C in permeabilized skeletal muscle. We show that cleavage leads to alterations in crossbridge kinetics and passive structural signatures of myofilaments that are indicative of a shift of myosin heads towards the ON state, highlighting the importance of MyBP-C<sup>C1C7</sup> to myofilament force production and regulation.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2025-04-26T12:02:50.515Z","creation":"2025-04-06T13:55:16.624Z"},"accession":"S-EPMC10960836","cross_references":{"pubmed":["38521794"],"doi":["10.1038/s41467-024-46957-7"]}}