{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Belyy V"],"funding":["Medical Research Council","Wellcome Trust","NIGMS NIH HHS"],"pagination":["1018-24"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5007201"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(9)"],"pubmed_abstract":["Kinesin and dynein motors transport intracellular cargos bidirectionally by pulling them in opposite directions along microtubules, through a process frequently described as a 'tug of war'. While kinesin produces 6 pN of force, mammalian dynein was found to be a surprisingly weak motor (0.5-1.5 pN) in vitro, suggesting that many dyneins are required to counteract the pull of a single kinesin. Mammalian dynein's association with dynactin and Bicaudal-D2 (BICD2) activates its processive motility, but it was unknown how this affects dynein's force output. Here, we show that formation of the dynein-dynactin-BICD2 (DDB) complex increases human dynein's force production to 4.3 pN. An in vitro tug-of-war assay revealed that a single DDB successfully resists a single kinesin. Contrary to previous "],"journal":["Nature cell biology"],"pubmed_title":["The mammalian dynein-dynactin complex is a strong opponent to kinesin in a tug-of-war competition."],"pmcid":["PMC5007201"],"funding_grant_id":["MC_UP_A025_1011","R01 GM094522","WT100387","100387"],"pubmed_authors":["Belyy V","Reimer AE","Carter AP","Schlager MA","Foster H","Yildiz A"],"additional_accession":[]},"is_claimable":false,"name":"The mammalian dynein-dynactin complex is a strong opponent to kinesin in a tug-of-war competition.","description":"Kinesin and dynein motors transport intracellular cargos bidirectionally by pulling them in opposite directions along microtubules, through a process frequently described as a 'tug of war'. While kinesin produces 6 pN of force, mammalian dynein was found to be a surprisingly weak motor (0.5-1.5 pN) in vitro, suggesting that many dyneins are required to counteract the pull of a single kinesin. Mammalian dynein's association with dynactin and Bicaudal-D2 (BICD2) activates its processive motility, but it was unknown how this affects dynein's force output. Here, we show that formation of the dynein-dynactin-BICD2 (DDB) complex increases human dynein's force production to 4.3 pN. An in vitro tug-of-war assay revealed that a single DDB successfully resists a single kinesin. Contrary to previous ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Sep","modification":"2026-04-17T15:30:32.678Z","creation":"2019-03-27T02:23:13Z"},"accession":"S-EPMC5007201","cross_references":{"pubmed":["27454819"],"doi":["10.1038/ncb3393"]}}