Yeast cells rely on the SPS-sensing pathway to respond to extracellular amino acids. This nutrient-induced signal transduction pathway regulates gene expression by controlling the activity of two redundant transcription factors: Stp1 and Stp2. These factors are synthesized as latent cytoplasmic proteins with N-terminal regulatory domains. Upon induction by extracellular amino acids, the plasma membrane SPS-sensor catalyses an endoproteolytic processing event that cleaves away the regulatory N-terminal domains. The shorter forms of Stp1 and Stp2 efficiently target to the nucleus, where they bind and activate transcription of selected genes encoding a subset of amino acid permeases that function at the plasma membrane to catalyse the transport of amino acids into cells. In the present article, the current understanding of events in the SPS-sensing pathway that enable external amino acids to induce their own uptake are reviewed with a focus on two key issues: (i) the maintenance of Stp1 and Stp2 latency in the absence of amino acid induction; and (ii) the amino-acid-induced SPS-sensor-mediated proteolytic cleavage of Stp1 and Stp2.
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February 2009
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Conference Article|
January 20 2009
Amino-acid-induced signalling via the SPS-sensing pathway in yeast
Per O. Ljungdahl
Per O. Ljungdahl
1
1Wenner-Gren Institute, Department of Cell Biology, S-10691 Stockholm, Sweden
1email plju@wgi.su.se
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Publisher: Portland Press Ltd
Received:
October 27 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (1): 242–247.
Article history
Received:
October 27 2008
Citation
Per O. Ljungdahl; Amino-acid-induced signalling via the SPS-sensing pathway in yeast. Biochem Soc Trans 1 February 2009; 37 (1): 242–247. doi: https://doi.org/10.1042/BST0370242
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