Immunoaffinity profiling of tyrosine phosphorylation in cancer cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-01-01

AUTHORS

John Rush, Albrecht Moritz, Kimberly A Lee, Ailan Guo, Valerie L Goss, Erik J Spek, Hui Zhang, Xiang-Ming Zha, Roberto D Polakiewicz, Michael J Comb

ABSTRACT

Tyrosine kinases play a prominent role in human cancer, yet the oncogenic signaling pathways driving cell proliferation and survival have been difficult to identify, in part because of the complexity of the pathways and in part because of low cellular levels of tyrosine phosphorylation. In general, global phosphoproteomic approaches reveal small numbers of peptides containing phosphotyrosine. We have developed a strategy that emphasizes the phosphotyrosine component of the phosphoproteome and identifies large numbers of tyrosine phosphorylation sites. Peptides containing phosphotyrosine are isolated directly from protease-digested cellular protein extracts with a phosphotyrosine-specific antibody and are identified by tandem mass spectrometry. Applying this approach to several cell systems, including cancer cell lines, shows it can be used to identify activated protein kinases and their phosphorylated substrates without prior knowledge of the signaling networks that are activated, a first step in profiling normal and oncogenic signaling networks. More... »

PAGES

94-101

Journal

TITLE

Nature Biotechnology

ISSUE

1

VOLUME

23

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1046

DOI

http://dx.doi.org/10.1038/nbt1046

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15592455


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