Evidence map›Paper›PMID 25425648›Full record

ArticleThe Journal of biological chemistry2015

Ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase (SCF) interact through multiple conformations.

Daniella Sandoval, Spencer Hill, Amy Ziemba, Steven Lewis, Brian Kuhlman, Gary Kleiger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  14. Suramin inhibits cullin-RING E3 ubiquitin ligases.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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 2 institutions in 1 country.

Daniella SandovalFrom the Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Nevada 89154-4003 and.
Spencer HillFrom the Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Nevada 89154-4003 and.
Amy ZiembaFrom the Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Nevada 89154-4003 and.
Steven Lewisthe Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260.
Brian Kuhlmanthe Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260.
Gary KleigerFrom the Department of Chemistry and Biochemistry, University of Nevada, Las Vegas, Nevada 89154-4003 and gary.kleiger@unlv.edu.
University of Nevada, Las Vegas · USUniversity of North Carolina at Chapel Hill · US

Funding

Outreach/Diversity/Pipeline ProjectP20GM103440 · NIGMS · UNIVERSITY OF NEVADA RENO · PI Eduardo A Robleto · 2012 to 2026
$58.0M
Designing Affinity and Specificity at Protein InterfacesR01GM073960 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A · 2005 to 2018
$3.1M
NIGMS NIH HHS P20 GM103440NIGMS NIH HHS R01 GM073960
6 · The paper itself

Abstract

In the ubiquitin-proteasome system, protein substrates are degraded via covalent modification by a polyubiquitin chain. The polyubiquitin chain must be assembled rapidly in cells, because a chain of at least four ubiquitins is required to signal for degradation, and chain-editing enzymes in the cell may cleave premature polyubiquitin chains before achieving this critical length. The ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase SCF are capable of building polyubiquitin chains onto protein substrates both rapidly and processively; this may be explained at least in part by the atypically fast rate of Cdc34 and SCF association. This rapid association has been attributed to electrostatic interactions between the acidic C-terminal tail of Cdc34 and a feature on SCF called the basic canyon. However, the structural aspects of the Cdc34-SCF interaction and how they permit rapid complex formation remain elusive. Here, we use protein cross-linking to demonstrate that the Cdc34-SCF interaction occurs in multiple conformations, where several residues from the Cdc34 acidic tail are capable of contacting a broad region of the SCF basic canyon. Similar patterns of cross-linking are also observed between Cdc34 and the Cul1 paralog Cul2, implicating the same mechanism for the Cdc34-SCF interaction in other members of the cullin-RING ubiquitin ligases. We discuss how these results can explain the rapid association of Cdc34 and SCF.

Indexed as

UbiquitinationAmino Acid SequenceAnaphase-Promoting Complex-CyclosomeCullin ProteinsHumansModels, MolecularProtein ConformationProtein Interaction Domains and MotifsProtein Structure, TertiarySKP Cullin F-Box Protein LigasesS-Phase Kinase-Associated ProteinsUbiquitinUbiquitin-Conjugating EnzymesAnaphase-Promoting Complex-CyclosomeCDC34 protein, humanCullin 1Cullin ProteinsSKP1 protein, humanSKP Cullin F-Box Protein LigasesS-Phase Kinase-Associated ProteinsUbiquitinUbiquitin-Conjugating EnzymesE3 Ubiquitin LigaseProtein-Protein InteractionUbiquitinUbiquitin-conjugating Enzyme (E2 Enzyme)Ubiquitylation (Ubiquitination)

Identifiers

PMID25425648
PMCPMC4294478
OpenAlexW2094538388

What OpenQuestion holds

Textmetadata
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.