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Genes & Dev. 20 (12): 1563-1568

Copyright © 2006 by Cold Spring Harbor Laboratory Press.


Regulation of transcription factor latency by receptor-activated proteolysis

Claes Andréasson1, Stijn Heessen, and Per O. Ljungdahl2

Ludwig Institute for Cancer Research, S-17177 Stockholm, Sweden

Abstract: The transcription factor Stp1 is endoproteolytically processed in response to extracellular amino acids by the plasma membrane SPS (Ssy1–Ptr3–Ssy5)-sensor. Processed Stp1, lacking a cytoplasmic retention motif, enters the nucleus and induces amino acid transporter gene expression. The SPS-sensor component Ssy5 is a chymotrypsin-like protease with a Pro-domain and a catalytic domain. The Pro-domain, required for protease maturation, is autolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex that binds Stp1. Stp1 is processed only after amino acid-induced signals cause the dissociation of the inhibitory Pro-domain. Our findings demonstrate that gene expression can be controlled by regulating the enzymatic activity of an intracellular endoprotease.

Key Words: Saccharomyces cerevisiae • environmental sensing • signal transduction • regulated proteolysis

Received for publication November 28, 2005. Accepted for publication April 6, 2006.

1 Present address: Zentrum für Molekulare Biologie Heidelberg, D-69120 Heidelberg, Germany.

2 Corresponding author.

E-MAIL plju{at}; FAX 46-8-33-28-12.

Supplemental Material is available at

Article is online at

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