Proteomic characterization of the human centrosome by protein correlation profiling

Jens S. Andersen, Christopher J. Wilkinson, Thibault Mayor, Peter Mortensen, Erich A. Nigg () and Matthias Mann ()
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Jens S. Andersen: University of Southern Denmark
Christopher J. Wilkinson: Max Planck Institute for Biochemistry
Thibault Mayor: Max Planck Institute for Biochemistry
Peter Mortensen: University of Southern Denmark
Erich A. Nigg: Max Planck Institute for Biochemistry
Matthias Mann: University of Southern Denmark

Nature, 2003, vol. 426, issue 6966, 570-574

Abstract: 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 cells1,2,3,4,5. 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.

Date: 2003
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DOI: 10.1038/nature02166

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