Phosphotyrosine mapping in oncogenic Bcr/Abl using phosphotyrosine specific immonium ion scanning

doi:10.1074/mcp.M300001-MCP200

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Submitted on January 9, 2003
Revised on February 25, 2003
Accepted on February 25, 2003

Phosphotyrosine mapping in oncogenic Bcr/Abl using phosphotyrosine specific immonium ion scanning

Hanno Steen, Minerva Fernandez, Saghi Ghaffari, Akhilesh Pandey, and Matthias Mann

Cell Biology, Harvard Medical School, Boston, MA 02115

Corresponding Author: hanno_steen{at}hms.harvard.edu

Bcr/Abl is a fusion oncoprotein that is of paramount importance in chronic myelogenous leukemia and acute lymphocytic leukemia. The tyrosine-phosphorylated fraction of p185 form of Bcr/Abl was isolated by immunoprecipitation with anti-phosphotyrosine antibodies and SDS-PAGE. The tryptic digest of the gel-separated protein was prefractionated on POROS R2/OLIGO R3 microcolumns and subjected to phosphotyrosine mapping by precursor ion scanning in positive ion mode utilizing the immonium ion of phosphotyrosine, also called phosphotyrosine specific immonium ion (PSI) scanning on a quadrupole TOF tandem mass spectrometer. In total, nine different phosphorylated tyrosine residues were unambiguously localized in twelve different precursor ions. These phosphorylation sites correspond to three previously described phosphotyrosine residues and six novel tyrosine phosphorylation sites, and most of them were not predicted by the phosphorylation motif prediction programs ProSite, NetPhos, or ScanSite. This study shows the power of PSI-scanning for sensitive phosphotyrosine mapping when limited amount of samples are available.

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