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Submitted on November 22, 2002
Revised on December 18, 2002
Accepted on January 6, 2003

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

Protein Laboratory, University of Copenhagen, Copenhagen 2200

Corresponding Author: hinsby{at}plab.ku.dk

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 (MS) 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 MS precursor ion scanning to identify twenty-two 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 Cgamma, 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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