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The fission yeast DNA structure checkpoint protein Rad26ATRIP/LCD1/UVSD accumulates in the cytoplasm following microtubule destabilization

Erin E Baschal, Kuan J Chen, Lee G Elliott, Matthew J Herring, Shawn C Verde and Tom D Wolkow*

Author Affiliations

University of Colorado at Colorado Springs, Department of Biology, 1420 Austin Bluffs Parkway, Colorado Springs, CO 80918, USA

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BMC Cell Biology 2006, 7:32  doi:10.1186/1471-2121-7-32

Published: 24 August 2006



DNA structure checkpoints are conserved eukaryotic signal transduction pathways that help preserve genomic integrity. Upon detecting checkpoint signals such as stalled replication forks or double-stranded DNA breaks, these pathways coordinate appropriate stress responses. Members of the PI-3 kinase related kinase (PIKK) family are essential elements of DNA structure checkpoints. In fission yeast, the Rad3 PIKK and its regulatory subunit Rad26 coordinate the detection of checkpoint signals with pathway outputs.


We found that untreated rad26Δ cells were defective for two microtubule-dependent processes: chromosome segregation and morphogenesis. Interestingly, cytoplasmic accumulation of Rad26-GFP occurred following treatment with microtubule destabilizing drugs, but not during treatment with the genotoxic agent Phleomycin. Cytoplasmic accumulation of Rad26-GFP depended on Rad24, a 14-3-3 protein also required for DNA structure checkpoints and morphogenesis. Results of over expression and epistasis experiments confirm that Rad26 and Rad24 define a response to microtubule destabilizing conditions.


Two DNA structure checkpoint proteins with roles in morphogenesis define a response to microtubule destabilizing conditions.