Accurate quantitation of protein expression and site-specific phosphorylation

Y. Oda, K. Huang, F. R. Cross, D. Cowburn, B. T. Chait

Research output: Contribution to journalArticlepeer-review

906 Scopus citations

Abstract

A mass spectrometry-based method is described for simultaneous identification and quantitation of individual proteins and for determining changes in the levels of modifications at specific sites on individual proteins. Accurate quantitation is achieved through the use of whole-cell stable isotope labeling. This approach was applied to the detection of abundance differences of proteins present in wild-type versus mutant cell populations and to the identification of in vivo phosphorylation sites in the PAK-related yeast Ste20 protein kinase that depend specifically on the G1 cyclin Cln2. The present method is general and affords a quantitative description of cellular differences at the level of protein expression and modification, thus providing information that is critical to the understanding of complex biological phenomena.

Original languageEnglish (US)
Pages (from-to)6591-6596
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number12
DOIs
StatePublished - Jun 8 1999
Externally publishedYes

ASJC Scopus subject areas

  • General

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