A systematic approach to the analysis of protein phosphorylation View Full Text


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Article Info

DATE

2001-04

AUTHORS

Huilin Zhou, Julian D. Watts, Ruedi Aebersold

ABSTRACT

Reversible protein phosphorylation has been known for some time to control a wide range of biological functions and activities1,2,3. Thus determination of the site(s) of protein phosphorylation has been an essential step in the analysis of the control of many biological systems. However, direct determination of individual phosphorylation sites occurring on phosphoproteins in vivo has been difficult to date, typically requiring the purification to homogeneity of the phosphoprotein of interest before analysis4,5,6. Thus, there has been a substantial need for a more rapid and general method for the analysis of protein phosphorylation in complex protein mixtures. Here we describe such an approach to protein phosphorylation analysis. It consists of three steps: (1) selective phosphopeptide isolation from a peptide mixture via a sequence of chemical reactions, (2) phosphopeptide analysis by automated liquid chromatography–tandem mass spectrometry (LC-MS/MS), and (3) identification of the phosphoprotein and the phosphorylated residue(s) by correlation of tandem mass spectrometric data with sequence databases. By utilizing various phosphoprotein standards and a whole yeast cell lysate, we demonstrate that the method is equally applicable to serine-, threonine- and tyrosine-phosphorylated proteins, and is capable of selectively isolating and identifying phosphopeptides present in a highly complex peptide mixture. More... »

PAGES

375-378

References to SciGraph publications

Journal

TITLE

Nature Biotechnology

ISSUE

4

VOLUME

19

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/86777

    DOI

    http://dx.doi.org/10.1038/86777

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1003596509

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11283598


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