Evidence map›Paper›PMID 38091999›Full record

ArticleMolecular cell2023

Bacterial ligases reveal fundamental principles of polyubiquitin specificity.

Tyler G Franklin, Peter S Brzovic, Jonathan N Pruneda

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Tyler G FranklinDepartment of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239, USA.
Peter S BrzovicDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Jonathan N PrunedaDepartment of Molecular Microbiology and Immunology, Oregon Health and Science University, Portland, OR 97239, USA. Electronic address: pruneda@ohsu.edu.
Oregon Health & Science University · USUniversity of Washington · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
Program in Molecular and Cellular BiosciencesT32GM071338 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MASLEN, CHERYL L · 2005 to 2020
$3.5M
Expanding Mechanistic Insights into Protein UbiquitylationR35GM144127 · NIGMS · UNIVERSITY OF WASHINGTON · PI Rachel E Klevit · 2022 to 2026
$3.2M
Exploiting bacterial effector proteins to study human ubiquitin signalingR35GM142486 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI Jonathan N Pruneda · 2021 to 2026
$2.6M
NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R35 GM142486NIGMS NIH HHS R35 GM144127NIGMS NIH HHS T32 GM071338
6 · The paper itself

Abstract

Homologous to E6AP C terminus (HECT) E3 ubiquitin (Ub) ligases direct substrates toward distinct cellular fates dictated by the specific form of monomeric or polymeric Ub (polyUb) signal attached. How polyUb specificity is achieved has been a long-standing mystery, despite extensive study in various hosts, ranging from yeast to human. The bacterial pathogens enterohemorrhagic Escherichia coli and Salmonella Typhimurium encode outlying examples of "HECT-like" (bHECT) E3 ligases, but commonalities to eukaryotic HECT (eHECT) mechanism and specificity had not been explored. We expanded the bHECT family with examples in human and plant pathogens. Three bHECT structures in primed, Ub-loaded states resolved key details of the entire Ub ligation process. One structure provided a rare glimpse into the act of ligating polyUb, yielding a means to rewire polyUb specificity of both bHECT and eHECT ligases. Studying this evolutionarily distinct bHECT family has revealed insight into the function of key bacterial virulence factors as well as fundamental principles underlying HECT-type Ub ligation.

Indexed as

PolyubiquitinUbiquitin-Protein LigasesHumansUbiquitinationPolyubiquitinUbiquitin-Protein Ligasesbacterial effectorE3 ubiquitin ligaseenterohemorrhagic Escherichia colipolyubiquitin specificitySalmonella TyphimuriumubiquitinX-ray crystallography

Identifiers

PMID38091999
PMCPMC10872931
OpenAlexW4389614059

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.