Evidence map›Paper›PMID 11673477›Full record

ArticleThe Journal of cell biology2001

Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.

S Vashist, W Kim, W J Belden, E D Spear, C Barlowe, D T Ng

Abstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
–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

108 citing papers in PubMed.

  1. Review
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  15. Trafficking-defective mutant PROKR2 cycles between endoplasmic reticulum and Golgi to attenuate endoplasmic reticulum stress.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  20. Review

48 more citing papers are in PubMed but not listed here.

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

6 authors.

S VashistDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.
W Kim
W J Belden
E D Spear
C Barlowe
D T Ng

Funding

Mechanisms of COPII-dependent TransportR01GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 1995 to 2024
$7.2M
Mechanisms of COPII-Dependent TransportR37GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 2007 to 2016
$5.3M
CELLULAR TOLERANCE MECHANISM OF ABERRANT PROTEINSR01GM059171 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI NG, DAVIS T.W. · 1999 to 2004
$1.1M
NIGMS NIH HHS GM052549NIGMS NIH HHS GM059171NIGMS NIH HHS R01 GM052549NIGMS NIH HHS R01 GM059171NIGMS NIH HHS R37 GM052549
6 · The paper itself

Abstract

Proteins destined for the secretory pathway must first fold and assemble in the lumen of endoplasmic reticulum (ER). The pathway maintains a quality control mechanism to assure that aberrantly processed proteins are not delivered to their sites of function. As part of this mechanism, misfolded proteins are returned to the cytosol via the ER protein translocation pore where they are ubiquitinated and degraded by the 26S proteasome. Previously, little was known regarding the recognition and targeting of proteins before degradation. By tracking the fate of several mutant proteins subject to quality control, we demonstrate the existence of two distinct sorting mechanisms. In the ER, substrates are either sorted for retention in the ER or are transported to the Golgi apparatus via COPII-coated vesicles. Proteins transported to the Golgi are retrieved to the ER via the retrograde transport system. Ultimately, both retained and retrieved proteins converge at a common machinery at the ER for degradation. Furthermore, we report the identification of a gene playing a novel role specific to the retrieval pathway. The gene, BST1, is required for the transport of misfolded proteins to the Golgi, although dispensable for the transport of many normal cargo proteins.

Indexed as

Protein FoldingAnimalsCells, CulturedCOP-Coated VesiclesEndoplasmic ReticulumGolgi ApparatusHN ProteinProtein TransportTime FactorsHN Protein

Identifiers

PMID11673477
PMCPMC2150856

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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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.