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Proteomic characterization of the human centrosome by protein correlation profiling
Author(s): Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M
Source: NATURE    Volume: 426    Issue: 6966    Pages: 570-574    Published: DEC 4 2003  
Times Cited: 361     References: 30     
Abstract: The centrosome is the major microtubule-organizing centre of animal cells and through its influence on the cytoskeleton is involved in cell shape, polarity and motility. It also has a crucial function in cell division because it determines the poles of the mitotic spindle that segregates duplicated chromosomes between dividing cells(1-5). Despite the importance of this organelle to cell biology and more than 100 years of study, many aspects of its function remain enigmatic and its structure and composition are still largely unknown. We performed a mass-spectrometry-based proteomic analysis of human centrosomes in the interphase of the cell cycle by quantitatively profiling hundreds of proteins across several centrifugation fractions. True centrosomal proteins were revealed by both correlation with already known centrosomal proteins and in vivo localization. We identified and validated 23 novel components and identified 41 likely candidates as well as the vast majority of the known centrosomal proteins in a large background of nonspecific proteins. Protein correlation profiling permits the analysis of any multiprotein complex that can be enriched by fractionation but not purified to homogeneity.
Document Type: Article
Language: English
Reprint Address: Nigg, EA (reprint author), Univ So Denmark, Dept Biochem & Mol Biol, Ctr Expt Bioinformat, Campusvej 55, DK-5230 Odense M, Denmark
Addresses:
1. Univ So Denmark, Dept Biochem & Mol Biol, Ctr Expt Bioinformat, DK-5230 Odense M, Denmark
2. Max Planck Inst Biochem, Dept Cell Biol, D-82152 Martinsried, Germany
Publisher: NATURE PUBLISHING GROUP, MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND
Subject Category: Multidisciplinary Sciences
IDS Number: 749TE
ISSN: 0028-0836
DOI: 10.1038/nature02166
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