{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sakamoto R"],"funding":["MEXT | Japan Society for the Promotion of Science","Human Frontier Science Program","Uehara Memorial Foundation","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["3444"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11043346"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Mechanical work serves as the foundation for dynamic cellular processes, ranging from cell division to migration. A fundamental driver of cellular mechanical work is the actin cytoskeleton, composed of filamentous actin (F-actin) and myosin motors, where force generation relies on adenosine triphosphate (ATP) hydrolysis. F-actin architectures, whether bundled by crosslinkers or branched via nucleators, have emerged as pivotal regulators of myosin II force generation. However, it remains unclear how distinct F-actin architectures impact the conversion of chemical energy to mechanical work. Here, we employ in vitro reconstitution of distinct F-actin architectures with purified components to investigate their influence on myosin ATP hydrolysis (consumption). We find that F-actin bundles compo"],"journal":["Nature communications"],"pubmed_title":["F-actin architecture determines the conversion of chemical energy into mechanical work."],"pmcid":["PMC11043346"],"funding_grant_id":["RGY0073/2018","U54 CA209992","R01 GM126256"],"pubmed_authors":["Murrell MP","Sakamoto R"],"additional_accession":[]},"is_claimable":false,"name":"F-actin architecture determines the conversion of chemical energy into mechanical work.","description":"Mechanical work serves as the foundation for dynamic cellular processes, ranging from cell division to migration. A fundamental driver of cellular mechanical work is the actin cytoskeleton, composed of filamentous actin (F-actin) and myosin motors, where force generation relies on adenosine triphosphate (ATP) hydrolysis. F-actin architectures, whether bundled by crosslinkers or branched via nucleators, have emerged as pivotal regulators of myosin II force generation. However, it remains unclear how distinct F-actin architectures impact the conversion of chemical energy to mechanical work. Here, we employ in vitro reconstitution of distinct F-actin architectures with purified components to investigate their influence on myosin ATP hydrolysis (consumption). We find that F-actin bundles compo","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-01T23:56:08.584Z","creation":"2026-05-24T03:07:31.101Z"},"accession":"S-EPMC11043346","cross_references":{"pubmed":["38658549"],"doi":["10.1038/s41467-024-47593-x"]}}