Evidence map›Paper›PMID 30560896›Full record

ArticleNature communications2018

The intralumenal fragment pathway mediates ESCRT-independent surface transporter down-regulation.

Erin Kate McNally, Christopher Leonard Brett

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  9. Autophagy in major human diseases.The EMBO journal · 2021
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Through the back door: Unconventional protein secretion.Cell surface (Amsterdam, Netherlands) · 2020
    Review
  16. ESCRT machinery plays a role in microautophagy in yeast.BMC molecular and cell biology · 2020
    Article
  17. Review
  18. Article
  19. Life in the lumen: The multivesicular endosome.Traffic (Copenhagen, Denmark) · 2020
    Review
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

2 authors at 1 institution in 1 country.

Erin Kate McNallyDepartment of Biology, Concordia University, 7141 Sherbrooke St. W., SP-501.15, Montréal, QC, H4R 1R6, Canada.
Christopher Leonard BrettDepartment of Biology, Concordia University, 7141 Sherbrooke St. W., SP-501.15, Montréal, QC, H4R 1R6, Canada. christopher.brett@concordia.ca.
Concordia University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Surface receptor and transporter protein down-regulation is assumed to be exclusively mediated by the canonical multivesicular body (MVB) pathway and ESCRTs (Endosomal Sorting Complexes Required for Transport). However, few surface proteins are known to require ESCRTs for down-regulation, and reports of ESCRT-independent degradation are emerging, suggesting that alternative pathways exist. Here, using Saccharomyces cerevisiae as a model, we show that the hexose transporter Hxt3 does not require ESCRTs for down-regulation conferring resistance to 2-deoxyglucose. This is consistent with GFP-tagged Hxt3 bypassing ESCRT-mediated entry into intralumenal vesicles at endosomes. Instead, Hxt3-GFP accumulates on vacuolar lysosome membranes and is sorted into an area that, upon fusion, is internalized as an intralumenal fragment (ILF) and degraded. Moreover, heat stress or cycloheximide trigger degradation of Hxt3-GFP and other surface transporter proteins (Itr1, Aqr1) by this ESCRT-independent process. How this ILF pathway compares to the MVB pathway and potentially contributes to physiology is discussed.

Indexed as

ProteolysisDeoxyglucoseDown-RegulationEndosomal Sorting Complexes Required for TransportEndosomesGlucose Transport Proteins, FacilitativeIntracellular MembranesLysosomesMultivesicular BodiesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionVacuolesDeoxyglucoseEndosomal Sorting Complexes Required for TransportGlucose Transport Proteins, FacilitativeHXT3 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID30560896
PMCPMC6299085
OpenAlexW2905351240

What OpenQuestion holds

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LicenceCC BY
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.