{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hessel AL"],"funding":["Deutsche Forschungsgemeinschaft","HHS | NIH | National Institute of General Medical Sciences","IZKF Muenster"],"pagination":["e2209441119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9860331"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(48)"],"pubmed_abstract":["Skeletal muscle force production is increased at longer compared to shorter muscle lengths because of length-dependent priming of thick filament proteins in the contractile unit before contraction. Using small-angle X-ray diffraction in combination with a mouse model that specifically cleaves the stretch-sensitive titin protein, we found that titin cleavage diminished the length-dependent priming of the thick filament. Strikingly, a titin-sensitive, length-dependent priming was also present in thin filaments, which seems only possible via bridge proteins between thick and thin filaments in resting muscle, potentially myosin-binding protein C. We further show that these bridges can be forcibly ruptured via high-speed stretches. Our results advance a paradigm shift to the fundamental regulation of length-dependent priming, with titin as the key driver."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Titin force in muscle cells alters lattice order, thick and thin filament protein formation."],"pmcid":["PMC9860331"],"funding_grant_id":["Li1/029/20","P30 GM138395","SFB1002 A08","P41 GM103622","454867250"],"pubmed_authors":["Rice PE","Linke WA","Nissen D","Kuehn M","Hessel AL","Mazara N","Irving T","Gong H","Ma W"],"additional_accession":[]},"is_claimable":false,"name":"Titin force in muscle cells alters lattice order, thick and thin filament protein formation.","description":"Skeletal muscle force production is increased at longer compared to shorter muscle lengths because of length-dependent priming of thick filament proteins in the contractile unit before contraction. Using small-angle X-ray diffraction in combination with a mouse model that specifically cleaves the stretch-sensitive titin protein, we found that titin cleavage diminished the length-dependent priming of the thick filament. Strikingly, a titin-sensitive, length-dependent priming was also present in thin filaments, which seems only possible via bridge proteins between thick and thin filaments in resting muscle, potentially myosin-binding protein C. We further show that these bridges can be forcibly ruptured via high-speed stretches. Our results advance a paradigm shift to the fundamental regulation of length-dependent priming, with titin as the key driver.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2025-04-04T08:06:24.912Z","creation":"2025-04-04T08:06:24.912Z"},"accession":"S-EPMC9860331","cross_references":{"pubmed":["36409887"],"doi":["10.1073/pnas.2209441119"]}}