{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lammers LG"],"funding":["NIGMS NIH HHS"],"pagination":["309-22"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4621840"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["211(2)"],"pubmed_abstract":["Cortically anchored dynein orients the spindle through interactions with astral microtubules. In budding yeast, dynein is offloaded to Num1 receptors from microtubule plus ends. Rather than walking toward minus ends, dynein remains associated with plus ends due in part to its association with Pac1/LIS1, an inhibitor of dynein motility. The mechanism by which dynein is switched from \"off\" at the plus ends to \"on\" at the cell cortex remains unknown. Here, we show that overexpression of the coiled-coil domain of Num1 specifically depletes dynein-dynactin-Pac1/LIS1 complexes from microtubule plus ends and reduces dynein-Pac1/LIS1 colocalization. Depletion of dynein from plus ends requires its microtubule-binding domain, suggesting that motility is required. An enhanced Pac1/LIS1 affinity mutan"],"journal":["The Journal of cell biology"],"pubmed_title":["The dynein cortical anchor Num1 activates dynein motility by relieving Pac1/LIS1-mediated inhibition."],"pmcid":["PMC4621840"],"funding_grant_id":["R01 GM118492"],"pubmed_authors":["Markus SM","Lammers LG"],"additional_accession":[]},"is_claimable":false,"name":"The dynein cortical anchor Num1 activates dynein motility by relieving Pac1/LIS1-mediated inhibition.","description":"Cortically anchored dynein orients the spindle through interactions with astral microtubules. In budding yeast, dynein is offloaded to Num1 receptors from microtubule plus ends. Rather than walking toward minus ends, dynein remains associated with plus ends due in part to its association with Pac1/LIS1, an inhibitor of dynein motility. The mechanism by which dynein is switched from \"off\" at the plus ends to \"on\" at the cell cortex remains unknown. Here, we show that overexpression of the coiled-coil domain of Num1 specifically depletes dynein-dynactin-Pac1/LIS1 complexes from microtubule plus ends and reduces dynein-Pac1/LIS1 colocalization. Depletion of dynein from plus ends requires its microtubule-binding domain, suggesting that motility is required. An enhanced Pac1/LIS1 affinity mutan","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2025-04-06T19:44:03.409Z","creation":"2019-03-27T02:00:49Z"},"accession":"S-EPMC4621840","cross_references":{"pubmed":["26483554"],"doi":["10.1083/jcb.201506119"]}}