Charting the protein complexome in yeast by mass spectrometry.
It has become evident over the past few years that many complex cellular processes, including control of the cell cycle and ubiquitin-dependent proteolysis, are carried out by sophisticated multisubunit protein machines that are dynamic in abundance, post-translational modification state, and composition. To understand better the nature of the macromolecular assemblages that carry out the cell cycle and ubiquitin-dependent proteolysis, we have used mass spectrometry extensively over the past few years to characterize both the composition of various protein complexes and the modification states of their subunits. In this article we review some of our recent efforts, and describe a promising new approach for using mass spectrometry to dissect protein interaction networks.
Deshaies
Raymond J
RJ
Divison of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125, USA. deshaies@its.caltech.edu
Seol
Jae Hong
JH
McDonald
W Hayes
WH
Cope
Greg
G
Lyapina
Svetlana
S
Shevchenko
Andrej
A
Shevchenko
Anna
A
Verma
Rati
R
Yates
John R
JR
D018797:Cell Cycle Proteins / Q000737:chemistry; D016208:Databases, Factual; D013058:Mass Spectrometry / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D013869:Thiolester Hydrolases / Q000737:chemistry*; D020798:Two-Hybrid System Techniques; D043222:Ubiquitin Thiolesterase
D018797:Cell Cycle Proteins; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D013869:Thiolester Hydrolases; D043222:Ubiquitin Thiolesterase