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Rapid degradation of the g(1) cyclin cln2 induced by cdk-dependent phosphorylation

Academic Article
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Overview

authors

  • Lanker, S.
  • Valdivieso, M. H.
  • Wittenberg, Curt

publication date

  • March 1996

journal

  • Science  Journal

abstract

  • Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.

subject areas

  • Amino Acid Sequence
  • CDC28 Protein Kinase, S cerevisiae
  • Cyclins
  • Enzyme Activation
  • Fungal Proteins
  • G1 Phase
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutation
  • Phenotype
  • Phosphorylation
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.271.5255.1597

PubMed ID

  • 8599119
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Additional Document Info

start page

  • 1597

end page

  • 1601

volume

  • 271

issue

  • 5255

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