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Dpb11 coordinates Mec1 kinase activationwith cell cycle-regulated Rad9 recruitment

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78499

Pfander,  Boris
Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society;

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emboj2011345a.pdf
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Zitation

Pfander, B., & Diffley, J. F. (2011). Dpb11 coordinates Mec1 kinase activationwith cell cycle-regulated Rad9 recruitment. The EMBO Journal, 30(24), 4897-4907. doi:10.1038/ emboj.2011.345.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-574C-C
Zusammenfassung
Eukaryotic cells respond to DNA damage by activating checkpoint signalling pathways. Checkpoint signals are transduced by a protein kinase cascade that also requires non-kinase mediator proteins. One such mediator is the Saccharomyces cerevisiae Dpb11 protein, which binds to and activates the apical checkpoint kinase, Mec1. Here, we show that a ternary complex of Dpb11, Mec1 and another key mediator protein Rad9 is required for efficient Rad9 phosphorylation by Mec1 in vitro, and for checkpoint activation in vivo. Phosphorylation of Rad9 by cyclindependent kinase (CDK) on two key residues generates a binding site for tandem BRCT repeats of Dpb11, and is thereby required for Rad9 recruitment into the ternary complex. Checkpoint signalling via Dpb11, therefore, does not efficiently occur during G1 phase when CDK is inactive. Thus, Dpb11 coordinates checkpoint signal transduction both temporally and spatially, ensuring the initiator kinase is specifically activated in proximity of one of its critical substrates.