{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Soppina P"],"funding":["Department of Science and Technology, Govt. of India","Department of Biotechnology, Ministry of Science and Technology, Govt. of India","Indian Council of Medical Research, Govt. of India","Science and Engineering Research Board, Department of Science and Technology, Government of India"],"pagination":["177"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9364601"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(1)"],"pubmed_abstract":["<h4>Background</h4>Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood.<h4>Results</h4>We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-"],"journal":["BMC biology"],"pubmed_title":["Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs."],"pmcid":["PMC9364601"],"funding_grant_id":["SR/WOS-A/LS-73/2017","BT/PR15214/BRB/10/1449/2015","5/13/13/2019/NCD-III","ECR/2016/000913","BT/RLF/Re-entry/45/2015"],"pubmed_authors":["Soppina V","Patel N","Naik PK","Soppina P","Sivaramakrishnan S","Rai A","Shewale DJ"],"additional_accession":[]},"is_claimable":false,"name":"Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.","description":"<h4>Background</h4>Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood.<h4>Results</h4>We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-04T22:35:54.284Z","creation":"2025-02-19T03:31:35.281Z"},"accession":"S-EPMC9364601","cross_references":{"pubmed":["35948971"],"doi":["10.1186/s12915-022-01370-8"]}}