Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-04

AUTHORS

Yoshiya Oda, Takeshi Nagasu, Brian T. Chait

ABSTRACT

The current progression from genomics to proteomics is fueled by the realization that many properties of proteins (e.g., interactions, post-translational modifications) cannot be predicted from DNA sequence1. Although it has become feasible to rapidly identify proteins from crude cell extracts using mass spectrometry after two-dimensional electrophoretic separation, it can be difficult to elucidate low-abundance proteins of interest in the presence of a large excess of relatively abundant proteins2,3. Therefore, for effective proteome analysis it becomes critical to enrich the sample to be analyzed in subfractions of interest. For example, the analysis of protein kinase substrates can be greatly enhanced by enriching the sample of phosphorylated proteins. Although enrichment of phosphotyrosine-containing proteins has been achieved through the use of high-affinity anti-phosphotyrosine antibodies4, the enrichment of phosphoserine/threonine-containing proteins has not been routinely possible. Here, we describe a method for enriching phosphoserine/threonine-containing proteins from crude cell extracts, and for subsequently identifying the phosphoproteins and sites of phosphorylation. The method, which involves chemical replacement of the phosphate moieties by affinity tags, should be of widespread utility for defining signaling pathways and control mechanisms that involve phosphorylation or dephosphorylation of serine/threonine residues. More... »

PAGES

379-382

Journal

TITLE

Nature Biotechnology

ISSUE

4

VOLUME

19

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/86783

    DOI

    http://dx.doi.org/10.1038/86783

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1026181446

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11283599


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