ArticleCommunications biology2025
Sae2 integrates CDK and checkpoint phosphorylation to coordinate MRX cleavage with checkpoint attenuation.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Yeast Sae2 plays a dual role in the DNA damage response by suppressing Rad53 activation and stimulating DNA end clipping via the MRX complex. Using AlphaFold3-based modeling and mutational analysis, here we show that Mec1/Tel1-dependent phosphorylation of Sae2 at T90 or T279 is sufficient to restrain Rad9-Rad53 interaction and Rad53 kinase activation. Cells expressing a non-phosphorylatable Sae2 double mutant (T90A T279A) display persistent Rad53 activation, whereas phosphomimetic Sae2 variants (T90E or T279E) restore normal checkpoint inactivation. Structural modeling and charge-reversal genetics indicate that electrostatic interactions between phosphorylated T90/T279 of Sae2 and Rad53 residue R70 are critical for this regulation. In addition, T279 phosphorylation, but not T90, cooperates with cyclin-dependent kinase (CDK)-dependent phosphorylation of Sae2 S267 to promote MRX-dependent resolution of hairpin DNA structures and processing of meiotic double-strand breaks (DSBs). A Sae2 T279E phosphomimetic partially rescues both hairpin cleavage defects and DNA damage sensitivity of tel1Δ cells, indicating that Tel1 promotes MRX activity primarily through Sae2 T279 phosphorylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.