Evidence map›Paper›PMID 30982603›Full record

ArticleCell2019

Redox State Controls Phase Separation of the Yeast Ataxin-2 Protein via Reversible Oxidation of Its Methionine-Rich Low-Complexity Domain.

Masato Kato, Yu-San Yang, Benjamin M Sutter, Yun Wang, Steven L McKnight, Benjamin P Tu

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

105 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
  7. Article
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45 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Masato KatoDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Yu-San YangDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Benjamin M SutterDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Yun WangDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Steven L McKnightDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA. Electronic address: steven.mcknight@utsouthwestern.edu.
Benjamin P TuDepartment of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA. Electronic address: benjamin.tu@utsouthwestern.edu.
Southwestern Medical CenterThe University of Texas Southwestern Medical Center · USSouthwestern Medical Center · US

Funding

A solid state conceptualization of information transfer from gene to message to proteinR35GM130358 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI STEVEN L MCKNIGHT · 2019 to 2026
$4.0M
METABOLIC SIGNALS DRIVING CELL GROWTH & PROLIFERATIONR01GM094314 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI TU, BENJAMIN P · 2010 to 2019
$3.2M
Reversible Polymerization of Low Complexity Polypeptide Sequences as a FrameworkU01GM107623 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MCKNIGHT, STEVEN L · 2014 to 2017
$2.0M
Laser Scanning Confocal for UT Southwestern Live Cell Imaging FacilityS10OD021684 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI LUBY-PHELPS, KATHERINE J · 2016 to 2016
$455k
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM094314NIGMS NIH HHS R35 GM130358NIGMS NIH HHS U01 GM107623NIH HHS S10 OD021684
6 · The paper itself

Abstract

Yeast ataxin-2, also known as Pbp1, senses the activity state of mitochondria in order to regulate TORC1. A domain of Pbp1 required to adapt cells to mitochondrial activity is of low sequence complexity. The low-complexity (LC) domain of Pbp1 forms labile, cross-β polymers that facilitate phase transition of the protein into liquid-like or gel-like states. Phase transition for other LC domains is reliant upon widely distributed aromatic amino acids. In place of tyrosine or phenylalanine residues prototypically used for phase separation, Pbp1 contains 24 similarly disposed methionine residues. Here, we show that the Pbp1 methionine residues are sensitive to hydrogen peroxide (H

Indexed as

Amino Acid SequenceCarrier ProteinsHydrogen PeroxideMechanistic Target of Rapamycin Complex 1MethionineMethionine Sulfoxide ReductasesMitochondriaMutagenesis, Site-DirectedOxidation-ReductionOxidative StressPhase TransitionProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsHydrogen PeroxideMechanistic Target of Rapamycin Complex 1Methioninemethionine sulfoxide reductaseMethionine Sulfoxide ReductasesPBP1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsagingAtaxin-2cross-β polymerlow-complexity sequencemethionineneurodegenerationoxidative stressphase separationROSTORC1

Identifiers

PMID30982603
PMCPMC6752730
OpenAlexW2936216122

What OpenQuestion holds

Textmetadata
LicenceTDM
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.