Proteomics

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K63-Linked Ubiquitylation of S2P-RNAPII Regulates Transcription in a DNA-PK Inter-Dependent Manner in Response to Double-Strand Breaks

ABSTRACT: DNA double-strand breaks (DSBs) pose a constant challenge to essential biological functions, including transcription, potentially leading to genomic instability. RNA polymerase II (RNAPII) plays a central role in detecting DNA lesions. Due to difficult-to-repair DSBs, RNAPII removal becomes challenging as it relies, among others, on multifaceted ubiquitylation mechanisms that are yet to be delineated. Our data suggests that during DSB repair, the E3 ubiquitin ligase NEDD4 as well as CRL3 complexes, albeit to a lesser extent, engage and catalyze the ubiquitylation of the elongating RNAPII, crafting a specific ubiquitin code for efficient repair. Specifically, NEDD4 is identified as the specific writer of K63-linked ubiquitin chains of S2P-RNAPII under stress as opposed to the total enzyme of RNAPII that is found to be modified mainly with K48 linkages. We find that these ligases, together with the ligase WWP2, exhibit a DNA-PK inter-dependency, driving proficient NHEJ repair and proper resolution of transcription defects caused by DSBs.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: iolanda Vendrell  

LAB HEAD: Tibor Pankotai

PROVIDER: PXD058988 | Pride | 2026-05-25

REPOSITORIES: Pride

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K63-linked ubiquitylation of S2P-RNAPII regulates transcription in a DNAPK inter-dependent manner in response to double-strand breaks.

Pantazi Vasiliki V   Smith Paul P   Pahi Zoltan G ZG   Katona Manuela M   Pap Adam A   Darula Zsuzsanna Z   Fischer Roman R   Vendrell Iolanda I   Kessler Benedikt M BM   van Vugt Marcel A T M MATM   D'Angiolella Vincenzo V   Pankotai Tibor T  

Nucleic acids research 20260401 8

DNA double-strand breaks (DSBs) are highly toxic DNA lesions that can lead to genomic instability. DSBs can also interfere with other DNA-based processes, including transcription, and thereby jeopardizing cellular function. In situations of persistent DSBs, RNA polymerase II (RNAPII) needs to be removed to facilitate DNA repair. DSB-induced RNAPII removal involves multifaceted ubiquitylation, but the mechanisms involved remain elusive. Our data show that in response to DSBs, the E3 ubiquitin lig  ...[more]

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