Evidence map›Paper›PMID 31166830›Full record

ArticleMolecular biology of the cell2019

Protein folding state-dependent sorting at the Golgi apparatus.

Doris Hellerschmied, Yevgeniy V Serebrenik, Lin Shao, George M Burslem, Craig M Crews

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

25 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  8. Article
  9. Review
  10. Article
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  13. Article
  14. Dysregulated proteostasis network in neuronal diseases.Frontiers in cell and developmental biology · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Protein quality control ofFrontiers in cellular neuroscience · 2022
    Review
  20. 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

5 authors.

Doris HellerschmiedDepartment of Molecular, Cellular and Developmental Biology.
Yevgeniy V SerebrenikDepartment of Molecular, Cellular and Developmental Biology.
Lin ShaoDepartment of Neuroscience, Yale School of Medicine, New Haven, CT 06520.
George M BurslemDepartment of Molecular, Cellular and Developmental Biology.
Craig M CrewsDepartment of Molecular, Cellular and Developmental Biology.

Funding

Inducing Proximity: An Emerging Paradigm for New Therapeutic ModalitiesR35CA197589 · NCI · YALE UNIVERSITY · PI CRAIG M CREWS · 2015 to 2026
$10.7M
NCI NIH HHS R35 CA197589
6 · The paper itself

Abstract

In eukaryotic cells, organelle-specific protein quality control (PQC) is critical for maintaining cellular homeostasis. Despite the Golgi apparatus being the major protein processing and sorting site within the secretory pathway, how it contributes to PQC has remained largely unknown. Using different chemical biology-based protein unfolding systems, we reveal the segregation of unfolded proteins from folded proteins in the Golgi. Quality control (QC) substrates are subsequently exported in distinct carriers, which likely contain unfolded proteins as well as highly oligomerized cargo that mimic protein aggregates. At an additional sorting step, oligomerized proteins are committed to lysosomal degradation, while unfolded proteins localize to the endoplasmic reticulum (ER) and associate with chaperones. These results highlight the existence of checkpoints at which QC substrates are selected for Golgi export and lysosomal degradation. Our data also suggest that the steady-state ER localization of misfolded proteins, observed for several disease-causing mutants, may have different origins.

Indexed as

alpha-MannosidaseAnimalsAntigens, CDbeta-D-Galactoside alpha 2-6-SialyltransferaseEndoplasmic ReticulumEukaryotic CellsGolgi ApparatusHEK293 CellsHeLa CellsHomeostasisHumansMiceMolecular ChaperonesProtein FoldingProtein TransportProtein Unfoldingalpha-MannosidaseAntigens, CDbeta-D-Galactoside alpha 2-6-SialyltransferaseMAN2A1 protein, ratMolecular ChaperonesSaccharomyces cerevisiae ProteinsSialyltransferasesST6GAL1 protein, human

Identifiers

PMID31166830
PMCPMC6743468

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.