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Article

Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling.

Molecular and cellular biology - 1 Sept 2003

Lee Soo-Jung, Schwartz Marc F, Duong Jimmy K, Stern David F

Abstract excerpt

Budding yeast Rad53 is an essential protein kinase that is phosphorylated and activated in a MEC1- and TEL1-dependent manner in response to DNA damage. We studied the role of Rad53 phosphorylation through mutation of consensus phosphorylation sites for upstream kinases Mec1 and Tel1. Alanine substitution of the Rad53 amino-terminal TQ cluster region reduced viability and impaired checkpoint functions. These...

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Identifiers

PMID: 12917350
DOI: 10.1128/MCB.23.17.6300-6314.2003
PMCID: PMC180918

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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