Review
Nature Reviews Molecular Cell Biology 6, 702-714 (September 2005) | doi:10.1038/nrm1711
Proteomics of organelles and large cellular structures
John R. Yates III1, Annalyn Gilchrist2, Kathryn E. Howell3 & John J. M. Bergeron2 About the authors
Summary
- Proteomics techniques have been successfully used to identify the protein components of organelles and large cellular structures.
- Several strategies have been developed that can be used to separate and identify the proteins in enriched organelle or subcellular fractions, and these include two-dimensional gel electrophoresis, one-dimensional SDS-PAGE and multidimensional liquid-chromatography–tandem mass spectrometry.
- Subtractive proteomics methods have been effective in highlighting the proteins that are specifically localized to organelles and other structures. However, it is difficult to identify the appropriate controls for these methods.
- Significant proteomics data have been accumulated for important organelles, such as mitochondria, the Golgi complex, the nuclear envelope, the endoplasmic reticulum and phagosomes.
- Large cellular structures such as the midbody, cytoskeleton and lipid rafts have also been successfully analysed using proteomics techniques.
Author affiliations
- Department of Cell Biology, 10550 North Torrey Pines Road, The Scripps Research Institute, La Jolla, California 92037, USA.
- Department of Anatomy and Cell Biology, Strathcona Anatomy and Dentistry Building, McGill University, Montreal, Quebec H3A 2B2, Canada.
- Department of Cell and Developmental Biology, Mail Stop 8108, University of Colorado School of Medicine at Fitzsimons, P.O. BOX 6511, Aurora, Colarado 80045, USA.
Correspondence to: John R. Yates III1 Email: jyates@scripps.edu
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