<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Sakamoto R</submitter><funding>MEXT | Japan Society for the Promotion of Science</funding><funding>Human Frontier Science Program</funding><funding>Uehara Memorial Foundation</funding><funding>NCI NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>3444</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11043346</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(1)</volume><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</pubmed_abstract><journal>Nature communications</journal><pubmed_title>F-actin architecture determines the conversion of chemical energy into mechanical work.</pubmed_title><pmcid>PMC11043346</pmcid><funding_grant_id>RGY0073/2018</funding_grant_id><funding_grant_id>U54 CA209992</funding_grant_id><funding_grant_id>R01 GM126256</funding_grant_id><pubmed_authors>Murrell MP</pubmed_authors><pubmed_authors>Sakamoto R</pubmed_authors></additional><is_claimable>false</is_claimable><name>F-actin architecture determines the conversion of chemical energy into mechanical work.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Apr</publication><modification>2026-06-01T23:56:08.584Z</modification><creation>2026-05-24T03:07:31.101Z</creation></dates><accession>S-EPMC11043346</accession><cross_references><pubmed>38658549</pubmed><doi>10.1038/s41467-024-47593-x</doi></cross_references></HashMap>