ArticleNucleic acids research2026
CTDP1 governs a Pol II phosphorylation intermediate and coordinates Mediator recruitment, transcription efficiency, and splicing.
Article in Nucleic acids research, 2026. 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
6 authors.
Funding
Abstract
RNA Pol II exists in hypo- (II-A) and hyper-phosphorylated (II-O) states on chromatin, which are linked to transcription initiation and elongation, respectively. Here, we identify a phosphorylation intermediate of Pol II (designated II-I) that is predominantly localized in the nucleoplasm and is enriched for phosphorylated Tyr1, Ser5, and Ser7 within the C-terminal domain (CTD). We demonstrate that the abundance of this phosphorylation intermediate is rapidly modulated by the phosphatase activity of CTDP1. Mechanistically, CTDP1-mediated regulation is critical for the recruitment of the Mediator complex to chromatin and for modulating Pol II transcriptional efficiency. Moreover, CTDP1's regulatory function extends to the dephosphorylation of splicing factors. Consequently, its depletion causes widespread intron retention and aberrant splicing of cassette exons. These findings position CTDP1 as a key regulator of Pol II phosphorylation intermediate and splicing regulation, with potential implications for cell cycle control.
Indexed as
Identifiers
What Socratic 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 Socratic graph.