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Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint.

Rad9 is required for the MEC1/TEL1-dependent activation of Saccharomyces cerevisiae DNA damage checkpoint pathways mediated by Rad53 and Chk1. DNA damage induces Rad9 phosphorylation, and Rad53 specifically associates with phosphorylated Rad9. We report here that multiple Mec1/Tel1 consensus [S/T]Q sites within Rad9 are phosphorylated in response to DNA damage. These Rad9 phosphorylation sites are selectively required for activation of the Rad53 branch of the checkpoint pathway. Consistent with the in vivo function in recruiting Rad53, Rad9 phosphopeptides are bound by Rad53 forkhead-associated (FHA) domains in vitro. These data suggest that functionally independent domains within Rad9 regulate Rad53 and Chk1, and support the model that FHA domain-mediated recognition of Rad9 phosphopeptides couples Rad53 to the DNA damage checkpoint pathway.

Pubmed ID: 12049741

Authors

  • Schwartz MF
  • Duong JK
  • Sun Z
  • Morrow JS
  • Pradhan D
  • Stern DF

Journal

Molecular cell

Publication Data

May 6, 2002

Associated Grants

  • Agency: NIDDK NIH HHS, Id: P01DK55389
  • Agency: NCI NIH HHS, Id: R01CA82257
  • Agency: NIGMS NIH HHS, Id: T32GM07223

Mesh Terms

  • Binding Sites
  • Cell Cycle Proteins
  • Checkpoint Kinase 2
  • DNA Damage
  • Forkhead Transcription Factors
  • Mutation
  • Nuclear Proteins
  • Phosphorylation
  • Protein Kinases
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors