4.8 Article

Integrated proteomic analysis of post-translational modifications by serial enrichment

Journal

NATURE METHODS
Volume 10, Issue 7, Pages 634-+

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nmeth.2518

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Funding

  1. Broad Institute of MIT and Harvard
  2. US National Institutes of Health from the National Cancer Institute Clinical Proteomics Tumor Analysis Consortium Initiative [U24CA160034]
  3. US National Institutes of Health from the National Heart, Lung, and Blood Institute [HHSN268201000033C, R01HL096738]

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We report a mass spectrometry-based method for the integrated analysis of protein expression, phosphorylation, ubiquitination and acetylation by serial enrichments of different post-translational modifications (SEPTM) from the same biological sample. This technology enabled quantitative analysis of nearly 8,000 proteins and more than 20,000 phosphorylation, 15,000 ubiquitination and 3,000 acetylation sites per experiment, generating a holistic view of cellular signal transduction pathways as exemplified by analysis of bortezomib-treated human leukemia cells.

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