Evidence map›Paper›PMID 24997600›Full record

ArticleNature structural & molecular biology2014

RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation.

Zuyao Ni, Chao Xu, Xinghua Guo, Gerald O Hunter, Olga V Kuznetsova, Wolfram Tempel, Edyta Marcon, Guoqing Zhong, Hongbo Guo, Wei-Hung William Kuo and 16 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
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

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.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed, 94 citations in OpenAlex.

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  16. ThrScience advances · 2024
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13 more citing papers are in PubMed but not listed here.

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

26 authors at 5 institutions in 3 countries.

Zuyao Ni *Donnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Chao Xu *Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Xinghua GuoDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Gerald O HunterDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Olga V KuznetsovaSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Wolfram TempelStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Edyta MarconDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Guoqing ZhongDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Hongbo GuoDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Wei-Hung William KuoDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Joyce LiDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Peter YoungDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Jonathan B OlsenDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Cuihong WanDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Peter LoppnauStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Majida El BakkouriStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Guillermo A SenisterraStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Hao HeStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Haiming HuangDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Sachdev S SidhuDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Andrew EmiliDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
Shona MurphySir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Amber L MosleyDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Cheryl H ArrowsmithStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Jinrong MinStructural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
Jack F GreenblattDonnelly Centre, University of Toronto, Toronto, Ontario, Canada.
University of Toronto · CAStructural Genomics Consortium · CAUniversity of Oxford · GBIndiana University – Purdue University Indianapolis · USIndiana University School of Medicine

Funding

Quality Assurance and Quality Control Project Management: Improving Submissions and Study Conduct in the Human Subjects Research Prior Approval ProcessUL1TR002529 · NCATS · INDIANA UNIVERSITY INDIANAPOLIS · PI MOE, SHARON M, WIEHE, SARAH ELIZABETH · 2018 to 2022
$27.2M
Indiana Clinical and Translational Sciences InstituteUL1TR001108 · NCATS · INDIANA UNIVERSITY INDIANAPOLIS · PI DENNE, SCOTT C., SHEKHAR, ANANTHA · 2013 to 2017
$23.3M
Regulation of RNA Polymerase II transcription by the phosphatase Rtr1R01GM099714 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI MOSLEY, AMBER L. · 2012 to 2021
$3.4M
CIHR MOP-258357Medical Research Council G0400653NCATS NIH HHS UL1 TR001108NIGMS NIH HHS GM099714NIGMS NIH HHS R01 GM099714Wellcome Trust 092483Wellcome Trust 092483/Z/10/ZWellcome Trust 092809Wellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal structures of the RPRD1A, RPRD1B and RPRD2 CIDs, alone and in complex with RNAPII CTD phosphoisoforms, elucidate the molecular basis of CTD recognition. In an example of cross-talk between different CTD modifications, our data also indicate that RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and, by interacting with CTD repeats where phospho-S2 and/or phospho-S7 bracket a phospho-S5 residue, serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAmino Acid SubstitutionCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayHEK293 CellsHumansHydrogen BondingModels, MolecularMolecular Sequence DataNeoplasm ProteinsPhosphorylationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationCarrier ProteinsCell Cycle ProteinsNeoplasm ProteinsRepressor ProteinsRNA Polymerase IIRPAP2 protein, humanRPRD1A protein, humanRPRD1B protein, humanSerine

Identifiers

PMID24997600
PMCPMC4124035
OpenAlexW2025727558

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.