Journal
CELL REPORTS
Volume 15, Issue 6, Pages 1242-1253Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2016.04.008
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Funding
- Ligue Nationale Contre le Cancer
- L'Institut National Du Cancer (TELOCHROM) [PLBIO14-012]
- Danish Council for Independent Research
- Villum Foundation
- European Research Council (ERCStG) [242905]
- Fundacao para a Ciencia e a Tecnologia
- Villum Fonden [00011407] Funding Source: researchfish
- European Research Council (ERC) [242905] Funding Source: European Research Council (ERC)
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In budding yeast, inactivation of telomerase and ensuing telomere erosion cause relocalization of telomeres to nuclear pore complexes (NPCs). However, neither the mechanism of such relocalization nor its significance are understood. We report that proteins bound to eroded telomeres are recognized by the SUMO (small ubiquitin-like modifier)-targeted ubiquitin ligase (STUbL) Slx5-Slx8 and become increasingly SUMOylated. Recruitment of Slx5-Slx8 to eroded telomeres facilitates telomere relocalization to NPCs and type II telomere recombination, a counterpart of mammalian alternative lengthening of telomeres (ALT). Moreover, artificial tethering of a telomere to a NPC promotes type II telomere recombination but cannot bypass the lack of Slx5-Slx8 in this process. Together, our results indicate that SUMOylation positively contributes to telomere relocalization to the NPC, where poly-SUMOylated proteins that accumulated over time have to be removed. We propose that STUbL-dependent relocalization of telomeres to NPCs constitutes a pathway in which excessively SUMOylated proteins are removed from congested'' intermediates to ensure unconventional recombination.
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