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Regulation and recognition of scfgrr1 targets in the glucose and amino acid signaling pathways

Academic Article
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Overview

authors

  • Spielewoy, N.
  • Flick, K.
  • Kalashnikova, T. I.
  • Walker, J. R.
  • Wittenberg, Curt

publication date

  • October 2004

journal

  • Molecular and Cellular Biology  Journal

abstract

  • 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.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Amino Acids
  • Casein Kinase I
  • Cyclins
  • F-Box Proteins
  • Gene Expression Regulation, Fungal
  • Glucose
  • Glucose Transport Proteins, Facilitative
  • Membrane Proteins
  • Monosaccharide Transport Proteins
  • Mutation
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Protein Structure, Tertiary
  • SKP Cullin F-Box Protein Ligases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
  • Ubiquitin
  • Ubiquitin-Protein Ligases
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Identity

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.24.20.8994-9005.2004

PubMed ID

  • 15456873
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Additional Document Info

start page

  • 8994

end page

  • 9005

volume

  • 24

issue

  • 20

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