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• W1976809737 endingPage "5923" @default.
• W1976809737 startingPage "5919" @default.
• W1976809737 abstract "Eukaryotic chromosome segregation depends on the mitotic spindle apparatus, a bipolar array of microtubules nucleated from centrosomes. Centrosomal microtubule nucleation requires attachment of γ-tubulin ring complexes to a salt-insoluble centrosomal core, but the factor(s) underlying this attachment remains unknown. In budding yeast, this attachment is provided by the coiled-coil protein Spc110p, which links the yeast γ-tubulin complex to the core of the yeast centrosome. Here, we show that the large coiled-coil protein kendrin is a human orthologue of Spc110p. We identified kendrin by its C-terminal calmodulin-binding site, which shares homology with the Spc110p calmodulin-binding site. Kendrin localizes specifically to centrosomes throughout the cell cycle. N-terminal regions of kendrin share significant sequence homology with pericentrin, a previously identified murine centrosome component known to interact with γ-tubulin. In mitotic human breast carcinoma cells containing abundant centrosome-like structures, kendrin is found only at centrosomes associated with spindle microtubules." @default.
• W1976809737 created "2016-06-24" @default.
• W1976809737 creator A5022826364 @default.
• W1976809737 creator A5049232635 @default.
• W1976809737 creator A5061090065 @default.
• W1976809737 creator A5075097036 @default.
• W1976809737 date "2000-05-23" @default.
• W1976809737 modified "2023-10-11" @default.
• W1976809737 title "Identification of a human centrosomal calmodulin-binding protein that shares homology with pericentrin" @default.
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• W1976809737 doi "https://doi.org/10.1073/pnas.97.11.5919" @default.
• W1976809737 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/18534" @default.
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