This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Spielewoy, N.
Right arrow Articles by Wittenberg, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Spielewoy, N.
Right arrow Articles by Wittenberg, C.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, October 2004, p. 8994-9005, Vol. 24, No. 20
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.20.8994-9005.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Regulation and Recognition of SCFGrr1 Targets in the Glucose and Amino Acid Signaling Pathways

Nathalie Spielewoy,1 Karin Flick,2 Tatyana I. Kalashnikova,1 John R. Walker,3 and Curt Wittenberg1,4*

Department of Molecular Biology,1 Department of Cell Biology, The Scripps Research Institute, La Jolla,4 Department of Biological Chemistry, University of California—Irvine, Irvine,2 RNA Dynamics Genomics Institute of the Novartis Foundation, San Diego, California3

Received 8 May 2004/ Returned for modification 31 May 2004/ Accepted 15 July 2004

SCFGrr1, one of several members of the SCF family of E3 ubiquitin ligases in budding Saccharomyces cerevisiae, is required for both regulation of the cell cycle and nutritionally controlled transcription. In addition to its role in degradation of Gic2 and the CDK targets Cln1 and Cln2, Grr1 is also required for induction of glucose- and amino acid-regulated genes. Induction of HXT genes by glucose requires the Grr1-dependent degradation of Mth1. We show that Mth1 is ubiquitinated in vivo and degraded via the proteasome. Furthermore, phosphorylated Mth1, targeted by the casein kinases Yck1/2, binds to Grr1. That binding depends upon the Grr1 leucine-rich repeat (LRR) domain but not upon the F-box or basic residues within the LRR that are required for recognition of Cln2 and Gic2. Those observations extend to a large number of Grr1-dependent genes, some targets of the amino acid-regulated SPS signaling system, which are properly regulated in the absence of those basic LRR residues. Finally, we show that regulation of the SPS targets requires the Yck1/2 casein kinases. We propose that casein kinase I plays a similar role in both nutritional signaling pathways by phosphorylating pathway components and targeting them for ubiquitination by SCFGrr1.

* Corresponding author. Mailing address: Department of Molecular Biology, MB-3, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 784-9628. Fax: (858) 784-2265. E-mail: curt{at}scripps.edu.

Molecular and Cellular Biology, October 2004, p. 8994-9005, Vol. 24, No. 20
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.20.8994-9005.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Xia, Z., Turner, G. C., Hwang, C.-S., Byrd, C., Varshavsky, A. (2008). Amino Acids Induce Peptide Uptake via Accelerated Degradation of CUP9, the Transcriptional Repressor of the PTR2 Peptide Transporter. J. Biol. Chem. 283: 28958-28968 [Abstract] [Full Text]  
  • Hnatova, M., Wesolowski-Louvel, M., Dieppois, G., Deffaud, J., Lemaire, M. (2008). Characterization of KlGRR1 and SMS1 Genes, Two New Elements of the Glucose Signaling Pathway of Kluyveromyces lactis. Eukaryot Cell 7: 1299-1308 [Abstract] [Full Text]  
  • Liu, Z., Thornton, J., Spirek, M., Butow, R. A. (2008). Activation of the SPS Amino Acid-Sensing Pathway in Saccharomyces cerevisiae Correlates with the Phosphorylation State of a Sensor Component, Ptr3. Mol. Cell. Biol. 28: 551-563 [Abstract] [Full Text]  
  • Varelas, X., Stuart, D., Ellison, M. J., Ptak, C. (2006). The Cdc34/SCF Ubiquitination Complex Mediates Saccharomyces cerevisiae Cell Wall Integrity. Genetics 174: 1825-1839 [Abstract] [Full Text]  
  • Santangelo, G. M. (2006). Glucose Signaling in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70: 253-282 [Abstract] [Full Text]  
  • Poulsen, P., Lo Leggio, L., Kielland-Brandt, M. C. (2006). Mapping of an Internal Protease Cleavage Site in the Ssy5p Component of the Amino Acid Sensor of Saccharomyces cerevisiae and Functional Characterization of the Resulting Pro- and Protease Domains by Gain-of-Function Genetics. Eukaryot Cell 5: 601-608 [Abstract] [Full Text]  
  • Kim, J.-H., Brachet, V., Moriya, H., Johnston, M. (2006). Integration of Transcriptional and Posttranslational Regulation in a Glucose Signal Transduction Pathway in Saccharomyces cerevisiae. Eukaryot Cell 5: 167-173 [Abstract] [Full Text]  
  • Eckert-Boulet, N., Larsson, K., Wu, B., Poulsen, P., Regenberg, B., Nielsen, J., Kielland-Brandt, M. C. (2006). Deletion of RTS1, Encoding a Regulatory Subunit of Protein Phosphatase 2A, Results in Constitutive Amino Acid Signaling via Increased Stp1p Processing. Eukaryot Cell 5: 174-179 [Abstract] [Full Text]  
  • Poulsen, P., Wu, B., Gaber, R. F., Kielland-Brandt, M. C. (2005). Constitutive Signal Transduction by Mutant Ssy5p and Ptr3p Components of the SPS Amino Acid Sensor System in Saccharomyces cerevisiae. Eukaryot Cell 4: 1116-1124 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»