Evidence map›Paper›PMID 31341161›Full record

ArticleNature communications2019

Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.

Katelyn M Williams, Shuo Qie, James H Atkison, Sabrina Salazar-Arango, J Alan Diehl, Shaun K Olsen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.5field-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

41 citing papers in PubMed, 64 citations in OpenAlex.

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  9. Review
  10. Article
  11. Review
  12. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  13. Article
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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 at 1 institution in 1 country.

Katelyn M WilliamsDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA.
Shuo QieDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA.
James H AtkisonDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA.
Sabrina Salazar-ArangoDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA.
J Alan DiehlDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA.ORCID http://orcid.org/0000-0001-9854-5049
Shaun K OlsenDepartment of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, 29425, USA. olsensk@musc.edu.ORCID http://orcid.org/0000-0002-1265-7101
Medical University of South Carolina · US

Funding

Transformed Esophageal Epithelial Cells and the Tumor MicroenvironmentP01CA098101 · NCI · UNIVERSITY OF PENNSYLVANIA · PI RUSTGI, ANIL K · 2003 to 2023
$31.7M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
T-COHR: Training in Craniofacial and Oral Health ResearchT32DE017551 · NIDCR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI YAO, HAI · 2006 to 2025
$10.3M
Nuclear Accumulation of D-type Cyclins and OncogenesisR01CA093237 · NCI · UNIVERSITY OF PENNSYLVANIA · PI DIEHL, JOHN ALAN · 2001 to 2022
$5.9M
Integrative Training in Oncogenic SignalingT32CA193201 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI HOWE, PHILIP H, LONG, DAVID THOMAS · 2016 to 2025
$3.7M
Structural Biology of the Ubiquitin Conjugation SystemR01GM115568 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI OLSEN, SHAUN · 2015 to 2023
$2.7M
MUSC Post-Baccalaureate Research Education ProgramR25GM113278 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DELEON-PENNELL, KRISTINE Y, PENROD-MARTIN, RACHEL · 2015 to 2024
$2.7M
Structure and Function of the Essential Cell Cycle Regulator Cdc34R01GM128731 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Shaun Olsen · 2019 to 2026
$2.5M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
MUSC Short-Term Research Education Program to Increase DiversityR25HL092611 · NHLBI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI WRIGHT, CYNTHIA F. · 2008 to 2022
$1.5M
Investigation of Cdc34 Molecular Recognition by its Enzyme Partners, Uba1 and SCF Ligases.F30CA216921 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI WILLIAMS, KATELYN · 2017 to 2020
$187k
Crystallization robotics to support X-ray crystallography at MUSCS10RR027139 · NCRR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI DAVIES, CHRISTOPHER · 2011 to 2011
$125k
NCI NIH HHS F30 CA216921NCI NIH HHS P01 CA098101NCI NIH HHS R01 CA093237NCI NIH HHS T32 CA193201NCRR NIH HHS S10 RR027139NCRR NIH HHS S10 RR029205NHLBI NIH HHS R25 HL092611NIDCR NIH HHS T32 DE017551NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM115568NIGMS NIH HHS R01 GM128731NIGMS NIH HHS R25 GM113278
6 · The paper itself

Abstract

Ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function. The molecular basis by which Cdc34 engages its E1 and the structural mechanisms by which its unique C-terminal extension functions in Cdc34 activity are unknown. Here, we present crystal structures of Cdc34 alone and in complex with E1, and a Cdc34~Ub thioester mimetic that represents the product of Uba1-Cdc34 Ub transthiolation. These structures reveal conformational changes in Uba1 and Cdc34 and a unique binding mode that are required for transthiolation. The Cdc34~Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34~Ub in a closed conformation and are critical for Ub discharge. Altogether, our structural, biochemical, and cell-based studies provide insights into the molecular mechanisms by which Cdc34 function in cells.

Indexed as

Cloning, MolecularCrystallography, X-RayHumansProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesCDC34 protein, humanCDC34 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUBA1 protein, humanUba1 protein, S cerevisiaeUbiquitin-Activating EnzymesUbiquitin-Conjugating Enzymes

Identifiers

PMID31341161
PMCPMC6656757
OpenAlexW2962948444

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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 OpenQuestion graph.