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- W2021351330 abstract "Cytoplasmic dynein functions at several sites during mitosis; however, the basis of targeting to each site remains unclear. Tandem mass spectrometry analysis of mitotic dynein revealed a phosphorylation site in the dynein intermediate chains (ICs) that mediates binding to kinetochores. IC phosphorylation directs binding to zw10 rather than dynactin, and this interaction is needed for kinetochore dynein localization. Phosphodynein associates with kinetochores from nuclear envelope breakdown to metaphase, but bioriented microtubule (MT) attachment and chromosome alignment induce IC dephosphorylation. IC dephosphorylation stimulates binding to dynactin and poleward streaming. MT depolymerization, release of kinetochore tension, and a PP1-γ mutant each inhibited IC dephosphorylation, leading to the retention of phosphodynein at kinetochores and reduced poleward streaming. The depletion of kinetochore dynactin by moderate levels of p50(dynamitin) expression disrupted the ability of dynein to remove checkpoint proteins by streaming at metaphase but not other aspects of kinetochore dynein activity. Together, these results suggest a new model for localization of kinetochore dynein and the contribution of kinetochore dynactin." @default.
- W2021351330 created "2016-06-24" @default.
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- W2021351330 date "2008-11-24" @default.
- W2021351330 modified "2023-09-25" @default.
- W2021351330 title "Phosphorylation regulates targeting of cytoplasmic dynein to kinetochores during mitosis" @default.
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- W2021351330 doi "https://doi.org/10.1083/jcb.200804114" @default.
- W2021351330 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2592828" @default.
- W2021351330 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19029334" @default.
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