BBS Faculty Member - Steven Gygi

Steven Gygi

Department of Cell Biology

Harvard Medical School
Seeley G. Mudd Building, Room 226
240 Longwood Avenue
Boston, MA 02115
Tel: 617-432-3155
Fax: 617-432-1144
Lab Members: 8 postdoctoral fellows, 3 graduate students

Technology drives biological research. A new technology can instantly provide answers that were difficult or impossible to address using current approaches. The emerging field of proteomics provides researchers an alternative/complementary strategy to the traditional genetic and biochemical approaches now used. Mass spectrometry is the enabling tool in proteomics and provides the ability to identify, characterize and even quantify differences at the protein level in cells and tissues. Landmark improvements in mass spectrometry-based proteomics allow for the comparative profiling of thousands of proteins in normal and disease states directly from complex mixtures (1). Finally, bioinformatics plays a major role in my lab to help fuel large-scale experiments (2).

One grant-funded project in the lab is to develop and apply methods for global phosphorylation analysis and quantification. We recently described a new approach to phosphorylation analysis where 2,002 sites of phosphorylation were detected on 900 proteins isolated from HeLa cell nuclei (3). We are now looking at cell cycle-specific phosphorylation events by profiling phosphorylation in synchronized yeast and HeLa cells.

A second major project in the lab is to develop mass spectrometry-based technologies to study protein ubiquitination. Ubiquitination is an extremely common posttranslational modification which in the past has been difficult to directly study because of the size of the modification (~8500 Da). In addition, polyubiquitin chains can be formed through either the traditional lysine 48 of ubiquitin or through any of six other alternative lysines present. A major goal of the lab is to unravel the biological function of each specific chain type using mass spectrometry and novel reagents called AQUA peptides (4).

Last Update: 8/22/2013


For a complete listing of publications click here.



Everley P.A., Bakalarski C.E., Elias J.E., Waghorne C.G., Beausoleil S.A., Gerber S.A., Faherty B.K., Zetter B.R., and Gygi S.P., An enhanced analysis of metastatic prostate cancer model using stable isotopes and high mass accuracy instrumentation. J. Proteome Res., 2006. In press.

Elias J.E., Gibbons F.D., King O.D., Roth F.P., and Gygi S.P., Intensity-based protein identification by machine learning from a library of tandem mass spectra. Nat Biotechnol, 2004. 22(2): p. 214-9.

Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., and Gygi S.P., Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A, 2004. 101(33): p. 12130-5.

Kirkpatrick D.S., Denison C., and Gygi S.P., Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nat Cell Biol, 2005. 7(8): p. 750-7.

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