The mass spectrometry analysis of CTDP1 function

ABSTRACT: We previously identified an interaction between the RNA polymerase II (Pol II) subunit RPB7 and the phosphatase CTDP1 in regulating transcription termination-reinitiation. Here, we establish that CTDP1 dephosphorylates a unique Pol II phospho-isoform modified at Tyr1, Ser5, and Ser7 of its C-terminal domain. This activity is critical for recruiting the Mediator complex and modulating transcriptional efficiency. Furthermore, by integrating phosphoproteomic and immunoprecipitation-mass spectrometry data, we reveal that CTDP1 also governs the phosphorylation of numerous RNA splicing factors. Our findings position CTDP1 as a master coordinator that integrates transcription with RNA splicing.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture, Embryonic Stem Cell

SUBMITTER: Haonan Zheng  

LAB HEAD: Xiong Ji

PROVIDER: PXD071392 | Pride | 2026-07-10

REPOSITORIES: Pride