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Molecular & Cellular Proteomics 2:29-36, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Signaling Initiated by Overexpression of the Fibroblast Growth Factor Receptor-1 Investigated by Mass Spectrometry^*

Anders M. Hinsby^,,¶, Jesper V. Olsen^,, Keiryn L. Bennett and Matthias Mann^,||

MDS Proteomics A/S, Staermosegaardsvej 6, Odense DK-5230, Denmark, the
Protein Laboratory, Institute of Molecular Pathology, Blegdamsvej 3, Panum Institute 6.2, University of Copenhagen, Copenhagen DK-2200, Denmark, and the
^|| Protein Interaction Laboratory, University of Southern Denmark, Campusvej 55, Odense DK-5230, Denmark

Overexpression of the fibroblast growth factor receptor-1 (FGFR-1), a prototypic receptor tyrosine kinase, is a feature of several human tumors. In human 293 cells overexpression of the FGFR-1 leads to constitutive activation of the receptor with concomitant sustained high increase in the cellular level of phosphotyrosine-containing proteins. Here we use mass spectrometry to study the tyrosine-phosphorylated proteins induced by overexpression of the FGFR-1. Several well known components of FGFR-1 signaling were identified along with two novel candidates: NS-1-associated protein-1 and target of Myb 1-like protein. We subsequently applied mass spectrometry precursor ion scanning to identify 22 tyrosine phosphorylation sites distributed on six substrate proteins of the FGFR-1 or downstream tyrosine kinases. Novel in vivo tyrosine phosphorylation sites were found in the FGFR-1, phospholipase C, p90 ribosomal S6 kinase, cortactin, and NS-1-associated protein-1 as a result of sustained FGFR-1 signaling, and we propose these as functional links to downstream molecular and cellular processes.

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