Identification of a human centrosomal calmodulin-binding protein that shares homology with pericentrin.

Eukaryotic chromosome segregation depends on the mitotic spindle apparatus, a bipolar array of microtubules nucleated from centrosomes. Centrosomal microtubule nucleation requires attachment of gamma-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 gamma-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 gamma-tubulin. In mitotic human breast carcinoma cells containing abundant centrosome-like structures, kendrin is found only at centrosomes associated with spindle microtubules.
Mesh Terms:
Antigens, Breast Neoplasms, Calmodulin, Calmodulin-Binding Proteins, Carcinoma, Centrosome, Cytoskeletal Proteins, Fibroblasts, Fungal Proteins, Gene Library, Humans, Microscopy, Fluorescence, Mitotic Spindle Apparatus, Molecular Sequence Data, Neoplasm Proteins, Nuclear Proteins, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Tubulin
Proc. Natl. Acad. Sci. U.S.A.
Date: May. 23, 2000
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