Evidence map›Paper›PMID 34047770›Full record

ArticleThe Journal of cell biology2021

ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation.

Xi Yang, Lucas Reist, Dominic A Chomchai, Liang Chen, Felichi Mae Arines, Ming Li

Open access · greenAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

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  8. IST1 regulates select recycling pathways.Traffic (Copenhagen, Denmark) · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Xi YangDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0003-2741-2294
Lucas Reist *Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0002-3990-5582
Dominic A Chomchai *Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0002-7697-2645
Liang ChenDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0002-7186-7109
Felichi Mae ArinesDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0002-5770-3116
Ming LiDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.ORCID 0000-0002-1247-2377
University of Michigan · US

Funding

Undergrad supplement: Ubiquitin-Dependent Protein Regulation and Quality Control of the Lysosomal MembraneR01GM133873 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LI, MING · 2019 to 2023
$1.9M
NIGMS NIH HHS R01 GM133873
6 · The paper itself

Abstract

The lysosome (or vacuole in fungi and plants) is an essential organelle for nutrient sensing and cellular homeostasis. In response to environmental stresses such as starvation, the yeast vacuole can adjust its membrane composition by selectively internalizing membrane proteins into the lumen for degradation. Regarding the selective internalization mechanism, two competing models have been proposed. One model suggests that the ESCRT machinery is responsible for the sorting. In contrast, the ESCRT-independent intralumenal fragment (ILF) pathway proposes that the fragment generated by homotypic vacuole fusion is responsible for the sorting. Here, we applied a microfluidics-based imaging method to capture the complete degradation process in vivo. Combining live-cell imaging with a synchronized ubiquitination system, we demonstrated that ILF cargoes are not degraded through intralumenal fragments. Instead, ESCRTs function on the vacuole membrane to sort them into the lumen for degradation. We further discussed challenges in reconstituting vacuole membrane protein degradation.

Indexed as

CeruloplasminEndosomal Sorting Complexes Required for TransportFerritinsGlucose Transport Proteins, FacilitativeIntracellular MembranesLysosomesMembrane ProteinsMicrofluidic Analytical TechniquesMicroscopy, FluorescenceProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime FactorsTime-Lapse ImagingUbiquitinationVacuolesCeruloplasminEndosomal Sorting Complexes Required for TransportFerritinsFET5 protein, S cerevisiaeGlucose Transport Proteins, FacilitativeHXT3 protein, S cerevisiaeMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID34047770
PMCPMC8167898
OpenAlexW3164581245

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.