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Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase by Stefan Gander; Debora Bonenfant; Patrick Altermatt; Dietmar E. Martin; Simon Hauri; Suzette Moes; Michael N. Hall; Paul Jenoe is a Chemistry article available to read on EtoBox.

What is Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase about?

## Abstract The __Saccharomyces cerevisae__ nitrogen permease reactivator Npr1 is a hyperphosphorylated protein that belongs to a fungus‐specific family of Ser/Thr protein kinases dedicated to the regulation of plasma membrane transporters. Its activity is regulated by the TOR (target of rapamycin) signalling pathway. Inhibition of the TOR proteins by treating yeast cells with the immunosuppressant drug rapamycin promotes rapid dephosphorylation of Npr1. To identify the rapamycin‐sensitive phosphorylation sites in yeast Npr1, glutathione‐S‐transferase (GST)‐tagged Npr1 was isolated from untreated or rapamycin‐treated cells, and analyzed by mass spectrometry. Here, we report for the first time 22 phosphorylation sites that are clustered in two regions of the N‐terminal serine‐rich domain. All phosphorylation sites, except two, were found to be rapamycin‐sensitive. Some phosphorylation sites are contained in motifs that closely resemble those in mammalian S6K (serines followed by a tyrosine or a phenylalanine) and 4E‐BP1 (serines followed by a proline). Other sites, such as serines followed by Ala, Asn, Gln, His, Ile, Leu, or Val, appear to define new motifs. Thus, TOR controls an un

Who reads Identification of the rapamycin-sensitive phosphorylation sites within the Ser/Thr-rich domain of the yeast Npr1 protein kinase?

Author

Stefan Gander; Debora Bonenfant; Patrick Altermatt; Dietmar E. Martin; Simon Hauri; Suzette Moes; Michael N. Hall; Paul Jenoe

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0951-4198)

Published

2008

Language

EN

Field

Chemistry (Physical Sciences)