NDLI: Deletion of RTS1, Encoding a Regulatory Subunit of Protein Phosphatase 2A, Results in Constitutive Amino Acid Signaling via Increased Stp1p Processing

Content Provider	PubMed Central
Author	Nadine, Eckert-boulet Larsson, Katrin Wu, Boqian Poulsen, Peter Regenberg, Birgitte Nielsen, Jens Kielland-brandt, Morten C.
Copyright Year	2006
Abstract	In Saccharomyces cerevisiae, extracellular amino acids are sensed at the plasma membrane by the SPS sensor, consisting of the transporter homologue Ssy1p, Ptr3p, and the endoprotease Ssy5p. Amino acid sensing results in proteolytic truncation of the transcription factors Stp1p and Stp2p, followed by their relocation from the cytoplasm to the nucleus, where they activate transcription of amino acid permease genes. We screened a transposon mutant library for constitutively signaling mutants, with the aim of identifying down-regulating components of the SPS-mediated pathway. Three isolated mutants were carrying a transposon in the RTS1 gene, which encodes a regulatory subunit of protein phosphatase 2A. We investigated the basal activity of the AGP1 and BAP2 promoters in rts1Δ cells and found increased transcription from these promoters, as well as increased Stp1p processing, even in the absence of amino acids. Based on our findings we propose that the phosphatase complex containing Rts1p keeps the SPS-mediated pathway down-regulated in the absence of extracellular amino acids by dephosphorylating a component of the pathway.
Related Links	http://dx.doi.org/10.1128/ec.5.1.174-179.2006
Ending Page	179
Page Count	6
Starting Page	174
File Format	PDF
ISSN	15359778
e-ISSN	15359786
Journal	Eukaryotic Cell
Issue Number	1
Volume Number	5
Language	English
Publisher	American Society for Microbiology
Publisher Date	2006-01-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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