Evidence map›Paper›PMID 28196862›Full record

ArticleThe Journal of biological chemistry2017

mTOR complex 1 activity is required to maintain the canonical endocytic recycling pathway against lysosomal delivery.

Kristin Dauner, Walaa Eid, Riya Raghupathy, John F Presley, Xiaohui Zha

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
1.5field-weighted citation impact, top 20% 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, 31 citations in OpenAlex.

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  18. mTORC1 activates SREBP-2 by suppressing cholesterol trafficking to lysosomes in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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

5 authors at 3 institutions in 2 countries.

Kristin DaunerFrom the Chronic Disease Program, Ottawa Hospital Research Institute and.
Walaa EidDepartment of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario K1H 8L6, Canada and.
Riya RaghupathyFrom the Chronic Disease Program, Ottawa Hospital Research Institute and.
John F Presleythe Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Xiaohui ZhaFrom the Chronic Disease Program, Ottawa Hospital Research Institute and xzha@ohri.ca.ORCID 0000-0003-2873-3073
Ottawa Hospital · CAUniversity of Ottawa · CAMcGill University · CA

Funding

CIHR MOP-130453
6 · The paper itself

Abstract

The plasma membrane of mammalian cells undergoes constitutive endocytosis, endocytic sorting, and recycling, which delivers nutrients to the lysosomes. The receptors, along with membrane lipids, are normally returned to the plasma membrane to sustain this action. It is not known, however, whether this process is influenced by metabolic conditions. Here we report that endocytic recycling requires active mechanistic target of rapamycin (aka mammalian target of rapamycin) (mTORC1), a master metabolic sensor. Upon mTORC1 inactivation, either by starvation or by inhibitor, recycling receptors and plasma membrane lipids, such as transferrin receptors and sphingomyelin, are delivered to the lysosomes. This lysosomal targeting is independent of canonical autophagy: both WT and Atg5

Indexed as

AnimalsAutophagy-Related Protein 5Biological Transport, ActiveCell ProliferationCells, CulturedEmbryo, MammalianEndocytosisEndosomal Sorting Complexes Required for TransportFibroblastsLysosomesMechanistic Target of Rapamycin Complex 1MiceMice, KnockoutMultiprotein ComplexesSphingomyelinsTOR Serine-Threonine KinasesAtg5 protein, mouseAutophagy-Related Protein 5Endosomal Sorting Complexes Required for TransportMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesSphingomyelinsTOR Serine-Threonine KinasesTransferrinautophagyendocytosisendosomal sorting complexes required for transport (ESCRT)Hrslysosomemembrane recyclingmTOR complex (mTORC)receptor recyclingtransferrin

Identifiers

PMID28196862
PMCPMC5392569
OpenAlexW2588907760

What OpenQuestion holds

Textmetadata
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.