Evidence map›Paper›PMID 22219383›Full record

ArticleMolecular biology of the cell2012

IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin.

Wei-Chieh Chiang, Carissa Messah, Jonathan H Lin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

57 citing papers in PubMed, 73 citations in OpenAlex.

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  11. Lysine Ubiquitylation Drives Rhodopsin Protein Turnover.Advances in experimental medicine and biology · 2023
    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

3 authors at 1 institution in 1 country.

Wei-Chieh ChiangDepartment of Pathology, University of California, San Diego, La Jolla, CA 92093, USA.
Carissa Messah
Jonathan H Lin
University of California San Diego · US

Funding

U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
Endoplasmic Reticulum Stress in Retinal DegenerationR01EY020846 · NEI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIN, JONATHAN · 2010 to 2014
$1.9M
Endoplasmic Reticulum Stress in Retinal DegenerationK08EY018313 · NEI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIN, JONATHAN · 2007 to 2011
$920k
NEI NIH HHS EY018313NEI NIH HHS EY020846NEI NIH HHS K08 EY018313NEI NIH HHS R01 EY020846NINDS NIH HHS P30 NS047101NINDS NIH HHS P30-NS047101
6 · The paper itself

Abstract

Endoplasmic reticulum (ER) is responsible for folding of secreted and membrane proteins in eukaryotic cells. Disruption of ER protein folding leads to ER stress. Chronic ER stress can cause cell death and is proposed to underlie the pathogenesis of many human diseases. Inositol-requiring enzyme 1 (IRE1) directs a key unfolded protein response signaling pathway that controls the fidelity of ER protein folding. IRE1 signaling may be particularly helpful in preventing chronic ER stress and cell injury by alleviating protein misfolding in the ER. To examine this, we used a chemical-genetic approach to selectively activate IRE1 in mammalian cells and tested how artificial IRE1 signaling affected the fate of misfolded P23H rhodopsin linked to photoreceptor cell death. We found that IRE1 signaling robustly promoted the degradation of misfolded P23H rhodopsin without affecting its wild-type counterpart. We also found that IRE1 used both proteasomal and lysosomal degradation pathways to remove P23H rhodopsin. Surprisingly, when one degradation pathway was compromised, IRE1 signaling could still promote misfolded rhodopsin degradation using the remaining pathway. Last, we showed that IRE1 signaling also reduced levels of several other misfolded rhodopsins with lesser effects on misfolded cystic fibrosis transmembrane conductance regulator. Our findings reveal the diversity of proteolytic mechanisms used by IRE1 to eliminate misfolded rhodopsin.

Indexed as

ProteolysisUnfolded Protein ResponseEndoplasmic ReticulumEndoplasmic Reticulum StressEndoribonucleasesHEK293 CellsHumansLysosomesMembrane ProteinsProteasome Endopeptidase ComplexProtein FoldingProtein Serine-Threonine KinasesRhodopsinEndoribonucleasesERN2 protein, humanMembrane ProteinsProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesRhodopsin

Identifiers

PMID22219383
PMCPMC3290636
OpenAlexW2132850971

What OpenQuestion holds

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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.