Evidence map›Paper›PMID 28978644›Full record

ArticleThe Journal of cell biology2017

Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers.

Yu Chen, David C Gershlick, Sang Yoon Park, Juan S Bonifacino

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 107 citations in OpenAlex.

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  5. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
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  8. Organelles harbour pH gradients.bioRxiv : the preprint server for biology · 2025
    Article
  9. Review
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  12. Article
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  15. Article
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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

4 authors at 1 institution in 1 country.

Yu ChenCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD.
David C GershlickCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD.ORCID 0000-0002-0602-210X
Sang Yoon ParkCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD.
Juan S BonifacinoCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD juan.bonifacino@nih.gov.ORCID 0000-0002-5673-6370
National Institutes of Health · US

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
Intramural NIH HHS ZIA HD001607
6 · The paper itself

Abstract

Biosynthetic sorting of newly synthesized transmembrane cargos to endosomes and lysosomes is thought to occur at the TGN through recognition of sorting signals in the cytosolic tails of the cargos by adaptor proteins, leading to cargo packaging into coated vesicles destined for the endolysosomal system. Here we present evidence for a different mechanism in which two sets of endolysosomal proteins undergo early segregation to distinct domains of the Golgi complex by virtue of the proteins' luminal and transmembrane domains. Proteins in one Golgi domain exit into predominantly vesicular carriers by interaction of sorting signals with adaptor proteins, but proteins in the other domain exit into predominantly tubular carriers shared with plasma membrane proteins, independently of signal-adaptor interactions. These findings demonstrate that sorting of endolysosomal proteins begins at an earlier stage and involves mechanisms that partly differ from those described by classical models.

Indexed as

Adaptor Protein Complex 2Amino Acid SequenceAntigens, CDCRISPR-Cas SystemsEndosomesGene ExpressionHeLa CellsHumansLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsLysosomesProtein Sorting SignalsProtein TransportReceptor, IGF Type 2Receptors, Transferrintrans-Golgi NetworkAdaptor Protein Complex 2Antigens, CDcation-dependent mannose-6-phosphate receptorCD71 antigenLAMP1 protein, humanLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsProtein Sorting SignalsReceptor, IGF Type 2Receptors, Transferrin

Identifiers

PMID28978644
PMCPMC5716290
OpenAlexW2760834034

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.