From a Complex Phosphoprotein to Complex Phosphoproteomes: The Role of Mass Spectrometry

Seminar

Title: From a Complex Phosphoprotein to Complex Phosphoproteomes: The Role of Mass Spectrometry

Speaker: Paul Jenö

Affiliation: Department of Biochemistry, Biozentrum of the University of Basel, Switzerland

Abstract:

In this seminar I will outline the role of mass spectrometry in tracking in vivo phosphorylation sites in proteins. As a first example, I shall discuss the influence protein phosphorylation has on the function of the yeast Npr1 kinase. Npr1 is a yeast protein kinase that actively supports sorting of the general amino acid permease Gap1 to the plasma membrane following nitrogen starvation. Upon nitrogen limitation, Npr1 becomes dephosphorylated and in turn activated. The function of Npr1 is poorly understood. I will present our approach in finding physiologically relevant substrates for Npr1 for deducing consensus sequences that can be used to predict bona fide substrates in yeast. In the second part I will demonstrate how quantitative phosphorylation analysis on a proteome wide level by mass spectrometry can be used to track hitherto unknown substrates for the yeast Tor kinases.

Short CV

From 1989 Head of Protein Chemistry/Mass Spectrometry Facility of the Biozentrum of the University of Basel

1987 - 1989 Research fellow at the Ludwig Institute for Cancer Research, London. Work on glycogen synthase kinase 3 (GSK3)

1984 – 1986 Postdoctoral fellow at the Cell Signalling Laboratory of the Friedrich Miescher Institute (FMI) (Dr. George Thomas). Work on ribosomal protein S6 kinase

1979 – 1983 PhD studies at the Biochemistry Department of the University of Berne

1975 – 1979　Biochemistry studies at the Federal Institute of Technology (ETH), Zurich, Switzerland