Identification of a human centrosomal calmodulin-binding protein that shares homology with pericentrin.
Proc Natl Acad Sci U S A
; 97(11): 5919-23, 2000 May 23.
Article
em En
| MEDLINE
| ID: mdl-10823944
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Ligação a Calmodulina
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Calmodulina
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Centrossomo
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Proteínas de Saccharomyces cerevisiae
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Antígenos
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Proteínas de Neoplasias
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article