Evidence map›Paper›PMID 27041596›Full record

ArticleStructure (London, England : 1993)2016

Structural Basis for Substrate Selectivity of the E3 Ligase COP1.

Sacha Uljon, Xiang Xu, Izabela Durzynska, Sarah Stein, Guillaume Adelmant, Jarrod A Marto, Warren S Pear, Stephen C Blacklow

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. A 32-bp deletion inHorticulture research · 2026
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  9. Review
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  11. Review
  12. TCP3 is a substrate of the COP1/SPA ubiquitin ligase to regulate anthocyanin accumulation and flowering time inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Review
  20. Article

3 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

8 authors at 4 institutions in 1 country.

Sacha UljonDepartment of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Xiang XuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Izabela DurzynskaDepartment of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Sarah SteinDepartment of Pathology and Laboratory Medicine, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.
Guillaume AdelmantDepartment of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Jarrod A MartoDepartment of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Warren S PearDepartment of Pathology and Laboratory Medicine, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.
Stephen C BlacklowDepartment of Cancer Biology, Dana Farber Cancer Institute, Boston, MA 02215, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA. Electronic address: stephen_blacklow@hms.harvard.edu.
Dana-Farber Cancer Institute · USHarvard University · USUniversity of Pennsylvania · USBrigham and Women's Hospital · US

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
IMMUNOBIOLOGY OF NORMAL AND NEOPLASTIC LYMPHOCYTEST32CA009140 · NCI · UNIVERSITY OF PENNSYLVANIA · PI Malay Haldar, WARREN S PEAR · 1985 to 2026
$16.1M
TRANSLATIONAL PHARMACOLOGY COREP50GM107618 · NIGMS · HARVARD MEDICAL SCHOOL · PI SORGER, PETER KARL · 2014 to 2018
$10.8M
Notch Regulation of Hematopoietic Cell FatesR01AI047833 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI JORDAN, MARTHA S, PEAR, WARREN S · 2000 to 2022
$7.4M
The Tribbles-COP1 Complex in LeukemiaK08CA166227 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ULJON, SACHA N · 2013 to 2017
$891k
NCI NIH HHS K08 CA166227NCI NIH HHS T32 CA009140NIAID NIH HHS R01 AI047833NIBIB NIH HHS P41 EB002026NIGMS NIH HHS P50 GM107618
6 · The paper itself

Abstract

COP1 proteins are E3 ubiquitin ligases that regulate phototropism in plants and target transcription factors for degradation in mammals. The substrate-binding region of COP1 resides within a WD40-repeat domain that also binds to Trib proteins, which are adaptors for C/EBPα degradation. Here we report structures of the human COP1 WD40 domain in isolation, and complexes of the human and Arabidopsis thaliana COP1 WD40 domains with the binding motif of Trib1. The human and Arabidopsis WD40 domains are seven-bladed β propellers with an inserted loop on the bottom face of the first blade. The Trib1 peptide binds in an extended conformation to a highly conserved surface on the top face of the β propeller, indicating a general mode for recognition of peptide motifs by COP1. Together, these studies identify the structural basis and key interactions for motif recognition by COP1, and hint at how Trib1 autoinhibition is overcome to target C/EBPα for degradation.

Indexed as

Molecular Docking SimulationArabidopsisArabidopsis ProteinsBinding SitesHumansIntracellular Signaling Peptides and ProteinsPeptide FragmentsProtein BindingProtein Serine-Threonine KinasesSubstrate SpecificityUbiquitin-Protein LigasesWD40 RepeatsArabidopsis ProteinsAT2G32950 protein, ArabidopsisCOP1 protein, humanIntracellular Signaling Peptides and ProteinsPeptide FragmentsProtein Serine-Threonine KinasesTRIB1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID27041596
PMCPMC4856590
OpenAlexW2316383613

What OpenQuestion holds

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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.