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First published online 17 February 2004
doi: 10.1242/jcs.00939
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Research Article |
1 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA
2 Deptartment of Biological Sciences, Stanford University, Stanford, CA 94305, USA
Author for correspondence (e-mail: angelab{at}stanford.edu)
Accepted 14 October 2003
Adenomatous polyposis coli (APC) and End-binding protein 1 (EB1) localize to centrosomes independently of cytoplasmic microtubules (MTs) and purify with centrosomes from mammalian cell lines. Localization of EB1 to centrosomes is independent of its MT binding domain and is mediated by its C-terminus. Both APC and EB1 preferentially localize to the mother centriole and EB1 forms a cap at the end of the mother centriole that contains the subdistal appendages as defined by 
-tubulin localization. Like endogenous APC and EB1, fluorescent protein fusions of APC and EB1 localize preferentially to the mother centriole. Depletion of EB1 by RNA interference reduces MT minus-end anchoring at centrosomes and delays MT regrowth from centrosomes. In summary, our data indicate that APC and EB1 are functional components of mammalian centrosomes and that EB1 is important for anchoring cytoplasmic MT minus ends to the subdistal appendages of the mother centriole.
Key words: Adenomatous polyposis coli, EB1, Centrosome, Mother centriole, Microtubule
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