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Pheromone-dependent destruction of the Tec1 transcription factor is required for MAP kinase signaling specificity in yeast

Academic Article
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Overview

authors

  • Bao, M. Z.
  • Schwartz, M. A.
  • Cantin, G. T.
  • Yates III, John
  • Madhani, H. D.

publication date

  • December 2004

journal

  • Cell  Journal

abstract

  • The yeast MAPK pathways required for mating versus filamentous growth share multiple components yet specify distinct programs. The mating-specific MAPK, Fus3, prevents crosstalk between the two pathways by unknown mechanisms. Here we show that pheromone signaling induces Fus3-dependent degradation of Tec1, the transcription factor specific to the filamentation pathway. Degradation requires Fus3 kinase activity and a MAPK phosphorylation site in Tec1 at threonine 273. Fus3 associates with Tec1 in unstimulated cells, and active Fus3 phosphorylates Tec1 on T273 in vitro. Destruction of Tec1 requires the F box protein Dia2 (Digs-into-agar-2), and Cdc53, the Cullin of SCF (Skp1-Cdc53-F box) ubiquitin ligases. Notably, mutation of the phosphoacceptor site in Tec1, deletion of FUS3, or deletion of DIA2 results in a loss of signaling specificity such that pheromone pathway signaling erroneously activates filamentation pathway gene expression and invasive growth. Signal-induced destruction of a transcription factor for a competing pathway provides a mechanism for signaling specificity.

subject areas

  • Amino Acid Sequence
  • Anaphase-Promoting Complex-Cyclosome
  • Cell Cycle Proteins
  • Cullin Proteins
  • DNA-Binding Proteins
  • F-Box Proteins
  • MAP Kinase Signaling System
  • Mitogen-Activated Protein Kinases
  • Molecular Sequence Data
  • Mutation
  • Pheromones
  • Phosphorylation
  • Protein Binding
  • SKP Cullin F-Box Protein Ligases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity
  • Threonine
  • Transcription Factors
  • Ubiquitin
  • Ubiquitin-Protein Ligase Complexes
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2004.11.052

PubMed ID

  • 15620357
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Additional Document Info

start page

  • 991

end page

  • 1000

volume

  • 119

issue

  • 7

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