Evidence map›Paper›PMID 41990034›Full record

ArticlePloS one2026

SHPRH together with the Ube2D family of enzymes directly ubiquitinates PCNA at Lys164 in vitro.

Xinyang Wang, Yixiong Hu, Yajiao Wen, Miaomiao Shen, Pu Chen, Song Xiang

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Article in PloS one, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Xinyang WangDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, Tianjin Medical University, Tianjin, P. R. CHINA.ORCID https://orcid.org/0000-0002-3929-2667
Yixiong HuDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, Tianjin Medical University, Tianjin, P. R. CHINA.
Yajiao WenDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, Tianjin Medical University, Tianjin, P. R. CHINA.
Miaomiao ShenTianjin Medical University Cancer Institute & Hospital, National Clinical Research Center for Cancer, Tianjin's Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin, P. R. CHINA.
Pu ChenDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, Tianjin Medical University, Tianjin, P. R. CHINA.
Song XiangDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, Tianjin Medical University, Tianjin, P. R. CHINA.ORCID https://orcid.org/0000-0001-9314-4684

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-chain attachment to a highly conserved Lys164 residue in the proliferating cell nuclear antigen (PCNA) signals for template switching events to resume stalled DNA replication. In human cells, the reaction is catalyzed by the ubiquitin ligases SNF2 histone linker PHD RING helicase (SHPRH) or helicase like transcription factor (HLTF), together with the Ubc13-Mms2 ubiquitin conjugating enzyme complex. The reaction requires mono-ubiquitinated PCNA as the substrate. Here, we provide biochemical evidence that SHPRH also directly ubiquitinates unmodified PCNA at Lys164. The reaction requires the Ube2D family of ubiquitin conjugating enzymes and robustly ubiquitinates both free and DNA-bound PCNA. We further found that efficient PCNA ubiquitination requires SHPRH's HIRAN domain, which mediate interactions with PCNA. Our data suggest another layer of regulation of DNA damage responses through PCNA ubiquitination.

Indexed as

DNA HelicasesLysineProliferating Cell Nuclear AntigenTranscription FactorsUbiquitinationUbiquitin-Conjugating EnzymesDNA-Binding ProteinsDNA DamageHumansProtein BindingUbiquitin-Protein LigasesDNA-Binding ProteinsDNA HelicasesHLTF protein, humanLysinePCNA protein, humanProliferating Cell Nuclear AntigenSHPRH protein, humanTranscription FactorsUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID41990034
PMCPMC13086300

What Socratic holds

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Registered trials

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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.