Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Subscribe

Logo for

J. Cell Biol. 173 (3): 327-331

Copyright © 2006 by the Rockefeller University Press.

Report

Competitive intra- and extracellular nutrient sensing by the transporter homologue Ssy1p

Boqian Wu, Kim Ottow, Peter Poulsen, Richard F. Gaber, Eva Albers, , and Morten C. Kielland-Brandt

Carlsberg Laboratory, DK-2500 Copenhagen, Denmark

Correspondence to Morten C. Kielland-Brandt: mkb{at}crc.dk

Abstract: Recent studies of Saccharomyces cerevisiae revealed sensors that detect extracellular amino acids (Ssy1p) or glucose (Snf3p and Rgt2p) and are evolutionarily related to the transporters of these nutrients. An intriguing question is whether the evolutionary transformation of transporters into nontransporting sensors reflects a homeostatic capability of transporter-like sensors that could not be easily attained by other types of sensors. We previously found SSY1 mutants with an increased basal level of signaling and increased apparent affinity to sensed extracellular amino acids. On this basis, we propose and test a general model for transporter- like sensors in which occupation of a single, central ligand binding site increases the activation energy needed for the conformational shift between an outward-facing, signaling conformation and an inward-facing, nonsignaling conformation. As predicted, intracellular leucine accumulation competitively inhibits sensing of extracellular amino acids. Thus, a single sensor allows the cell to respond to changes in nutrient availability through detection of the relative concentrations of intra- and extracellular ligand.

K. Ottow's present address is Technical University of Denmark, DK-2800 Lyngby, Denmark.

P. Poulsen's present address is University of Copenhagen, DK-1017 Copenhagen, Denmark.

R.F. Gaber's present address Northwestern University, Evanston, IL 60208.

E. Albers's present address is Chalmers University of Technology, SE-412 96 Göteborg, Sweden.

Abbreviation used in this paper: DW, dry weight.

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Rts1-protein phosphatase 2A antagonizes Ptr3-mediated activation of the signaling protease Ssy5 by casein kinase I.
D. J. Omnus and P. O. Ljungdahl (2013)
Mol. Biol. Cell 24, 1480-1492
   Abstract »    Full Text »    PDF »
Nutritional Control of Growth and Development in Yeast.
J. R. Broach (2012)
Genetics 192, 73-105
   Abstract »    Full Text »    PDF »
Regulation of Amino Acid, Nucleotide, and Phosphate Metabolism in Saccharomyces cerevisiae.
P. O. Ljungdahl and B. Daignan-Fornier (2012)
Genetics 190, 885-929
   Abstract »    Full Text »    PDF »
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase.
R. Zoncu, L. Bar-Peled, A. Efeyan, S. Wang, Y. Sancak, and D. M. Sabatini (2011)
Science 334, 678-683
   Abstract »    Full Text »    PDF »
A phosphodegron controls nutrient-induced proteasomal activation of the signaling protease Ssy5.
D. J. Omnus, T. Pfirrmann, C. Andreasson, and P. O. Ljungdahl (2011)
Mol. Biol. Cell 22, 2754-2765
   Abstract »    Full Text »    PDF »
Transport activity-dependent intracellular sorting of the yeast general amino acid permease.
N. E. Cain and C. A. Kaiser (2011)
Mol. Biol. Cell 22, 1919-1929
   Abstract »    Full Text »    PDF »
The Prodomain of Ssy5 Protease Controls Receptor-Activated Proteolysis of Transcription Factor Stp1.
T. Pfirrmann, S. Heessen, D. J. Omnus, C. Andreasson, and P. O. Ljungdahl (2010)
Mol. Cell. Biol. 30, 3299-3309
   Abstract »    Full Text »    PDF »
Transport and signaling through the phosphate-binding site of the yeast Pho84 phosphate transceptor.
Y. Popova, P. Thayumanavan, E. Lonati, M. Agrochao, and J. M. Thevelein (2010)
PNAS 107, 2890-2895
   Abstract »    Full Text »    PDF »
Amino Acid Signaling in Yeast: Post-genome Duplication Divergence of the Stp1 and Stp2 Transcription Factors.
K. Wielemans, C. Jean, S. Vissers, and B. Andre (2010)
J. Biol. Chem. 285, 855-865
   Abstract »    Full Text »    PDF »
Functioning and Evolutionary Significance of Nutrient Transceptors.
J. M. Thevelein and K. Voordeckers (2009)
Mol. Biol. Evol. 26, 2407-2414
   Abstract »    Full Text »    PDF »
GLUT2 mutations, translocation, and receptor function in diet sugar managing.
A. Leturque, E. Brot-Laroche, and M. Le Gall (2009)
Am J Physiol Endocrinol Metab 296, E985-E992
   Abstract »    Full Text »    PDF »
Amino acid regulation of TOR complex 1.
J. Avruch, X. Long, S. Ortiz-Vega, J. Rapley, A. Papageorgiou, and N. Dai (2009)
Am J Physiol Endocrinol Metab 296, E592-E602
   Abstract »    Full Text »    PDF »
Inhibition of SNAT2 by Metabolic Acidosis Enhances Proteolysis in Skeletal Muscle.
K. Evans, Z. Nasim, J. Brown, E. Clapp, A. Amin, B. Yang, T. P. Herbert, and A. Bevington (2008)
J. Am. Soc. Nephrol. 19, 2119-2129
   Abstract »    Full Text »    PDF »
Amino Acids Induce Peptide Uptake via Accelerated Degradation of CUP9, the Transcriptional Repressor of the PTR2 Peptide Transporter.
Z. Xia, G. C. Turner, C.-S. Hwang, C. Byrd, and A. Varshavsky (2008)
J. Biol. Chem. 283, 28958-28968
   Abstract »    Full Text »    PDF »
Dal81 Enhances Stp1- and Stp2-Dependent Transcription Necessitating Negative Modulation by Inner Nuclear Membrane Protein Asi1 in Saccharomyces cerevisiae.
M. Boban and P. O. Ljungdahl (2007)
Genetics 176, 2087-2097
   Abstract »    Full Text »    PDF »
Distinct Sensor Pathways in the Hierarchical Control of SNAT2, a Putative Amino Acid Transceptor, by Amino Acid Availability.
R. Hyde, E. L. Cwiklinski, K. MacAulay, P. M. Taylor, and H. S. Hundal (2007)
J. Biol. Chem. 282, 19788-19798
   Abstract »    Full Text »    PDF »
Glutamate in plants: metabolism, regulation, and signalling.
B. G. Forde and P. J. Lea (2007)
J. Exp. Bot. 58, 2339-2358
   Abstract »    Full Text »    PDF »
Identification of an N-Acetylglucosamine Transporter That Mediates Hyphal Induction in Candida albicans.
F. J. Alvarez and J. B. Konopka (2007)
Mol. Biol. Cell 18, 965-975
   Abstract »    Full Text »    PDF »
Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors.
M. Boban, A. Zargari, C. Andreasson, S. Heessen, J. Thyberg, and P. O. Ljungdahl (2006)
J. Cell Biol. 173, 695-707
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882