Proteomic characterization of the human centrosome by protein correlation profiling
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. 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.
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High mass resolution is crucial to accurate quantification because accurate determination of XICs of peptides is critical for comparison between samples.
“Although high mass accuracy aids in the identification of peptides (42), it is the high mass resolution that is crucial to accurate quantification. This is because the accurate determination of extracted ion currents (XICs) of peptides is critical for comparison between samples (43).”
From Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ (2014) · cites this paper as [43]
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- Authors
- Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., & Mann, M.
- Affiliations
- University of Southern Denmark (DK)
- Max Planck Institute of Biochemistry (DE)
- Corresponding author
- Nigg, Erich A.
- Mann, Matthias
- Venue
- Nature
- Published
- 2003-12
- Volume
- 426
- Issue
- 6966
- Pages
- 570-574
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2162681116
- Cited by
- 1,319
- References
- 30
- Citations by year
- 2026: 18 · 2025: 34 · 2024: 26 · 2023: 33 · 2022: 45 · 2021: 55 · 2020: 41 · 2019: 52 · 2018: 43 · 2017: 42 · 2016: 56 · 2015: 57 · 2014: 63 · 2013: 56 · 2012: 92
- FWCI
- 29.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- centrosome, centrosomal proteins, microtubule organizing center, mitotic spindle, protein complex composition
- MeSH terms
- Amino Acid Sequence, Cell Line, Cloning, Molecular, Humans, Interphase, Molecular Sequence Data, Proteins, Mass Spectrometry, Substrate Specificity, Centrosome, Gene Expression Profiling, Proteomics
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