Evidence map›Paper›PMID 20159592›Full record

ArticleDevelopmental cell2010

Structural basis of selective ubiquitination of TRF1 by SCFFbx4.

Zhixiong Zeng, Wei Wang, Yuting Yang, Yong Chen, Xiaomei Yang, J Alan Diehl, Xuedong Liu, Ming Lei

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones.SLAS discovery : advancing life sciences R & D · 2021
    Review
  7. Review
  8. Review
  9. Article
  10. Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCFProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Expression, purification and crystallization of the FP domain of the human F-box protein Fbxo7.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  20. Mechanisms and function of substrate recruitment by F-box proteins.Nature reviews. Molecular cell biology · 2013
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Zhixiong ZengHoward Hughes Medical Institute, University of Michigan Medical School, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA.
Wei Wang
Yuting Yang
Yong Chen
Xiaomei Yang
J Alan Diehl
Xuedong Liu
Ming Lei
Howard Hughes Medical Institute · USUniversity of Colorado Boulder · USShandong University · CNUniversity of Pennsylvania · US

Funding

Mechanisms of p27Kipl Proteolysis in Cancer CellsR01CA107098 · NCI · UNIVERSITY OF COLORADO AT BOULDER · PI LIU, XUEDONG · 2004 to 2012
$2.7M
Structure of the Telomere Shelterin ComplexR01GM083015 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LEI, MING · 2008 to 2012
$1.2M
Howard Hughes Medical InstituteNCI NIH HHS CA 107098NCI NIH HHS R01 CA107098NCI NIH HHS Y1-CO-1020NIGMS NIH HHS GM 083015-01NIGMS NIH HHS R01 GM083015NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

TRF1 is a critical regulator of telomere length. As such, TRF1 levels are regulated by ubiquitin-dependent proteolysis via an SCF E3 ligase where Fbx4 contributes to substrate specification. Here, we report the crystal structure of the Fbx4-TRF1 complex at 2.4 A resolution. Fbx4 contains an unusual substrate-binding domain that adopts a small GTPase fold. Strikingly, this atypical GTPase domain of Fbx4 binds to a globular domain of TRF1 through an intermolecular beta sheet, instead of recognizing short peptides/degrons as often seen in other F-box protein-substrate complexes. Importantly, mutations in this interface abrogate Fbx4-dependent TRF1 binding and ubiquitination. Furthermore, the data demonstrate that recognition of TRF1 by SCF(Fbx4) is regulated by another telomere protein, TIN2. Our results reveal an atypical small GTPase domain within Fbx4 as a substrate-binding motif for SCF(Fbx4) and uncover a mechanism for selective ubiquitination and degradation of TRF1 in telomere homeostasis control.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesCell LineCrystallography, X-RayHomeostasisHumansIn Vitro TechniquesModels, MolecularMonomeric GTP-Binding ProteinsMultiprotein ComplexesMutationProtein Processing, Post-TranslationalProtein StabilityProtein Structure, TertiaryRecombinant Fusion ProteinsMonomeric GTP-Binding ProteinsMultiprotein ComplexesRecombinant Fusion ProteinsRNA, Small InterferingSKP Cullin F-Box Protein LigasesTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1TINF2 protein, human

Identifiers

PMID20159592
PMCPMC6097615
OpenAlexW2014896987

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.