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

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.

• Authors: M R Flory, M J Moser, R J Monnat Jr, T N Davis
• Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 97 Issue 11 Pg. 5919-23 (May 23 2000) ISSN: 0027-8424 [Print] United States
• PMID: 10823944 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antigens
• Calmodulin
• Calmodulin-Binding Proteins
• Cytoskeletal Proteins
• Fungal Proteins
• Neoplasm Proteins
• Nuclear Proteins
• Recombinant Fusion Proteins
• SPC110 protein, S cerevisiae
• Saccharomyces cerevisiae Proteins
• Tubulin
• kendrin
• pericentrin

Topics

• Antigens (chemistry)
• Breast Neoplasms (genetics, metabolism, pathology)
• Calmodulin (metabolism)
• Calmodulin-Binding Proteins (chemistry, genetics, isolation & purification)
• Carcinoma (genetics, metabolism, pathology)
• Centrosome (metabolism)
• Cytoskeletal Proteins
• Fibroblasts (metabolism)
• Fungal Proteins (chemistry)
• Gene Library
• Humans
• Microscopy, Fluorescence
• Molecular Sequence Data
• Neoplasm Proteins (chemistry, genetics, isolation & purification)
• Nuclear Proteins (chemistry)
• Recombinant Fusion Proteins (metabolism)
• Saccharomyces cerevisiae (metabolism)
• Saccharomyces cerevisiae Proteins
• Sequence Alignment
• Sequence Homology, Amino Acid
• Species Specificity
• Spindle Apparatus (metabolism)
• Tubulin (metabolism)