Evidence map›Paper›PMID 28589942›Full record

ArticleNature communications2017

Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex.

Joori Park, Yeonkyoung Park, Incheol Ryu, Mi-Hyun Choi, Hyo Jin Lee, Nara Oh, Kyutae Kim, Kyoung Mi Kim, Junho Choe, Cheolju Lee and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Joori ParkCreative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea.
Yeonkyoung ParkCreative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea.
Incheol RyuCreative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea.
Mi-Hyun ChoiDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
Hyo Jin LeeDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
Nara OhCreative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea.
Kyutae KimDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
Kyoung Mi KimDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
Junho ChoeDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.
Cheolju LeeBRI, Korea Institute of Science and Technology, Hwarangno 14-gil 5, Seongbuk-gu, Seoul 02792, Republic of Korea.
Ja-Hyun BaikDivision of Life Sciences, Korea University, Seoul 02841, Republic of Korea.ORCID 0000-0002-4607-924X
Yoon Ki KimCreative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Misfolded polypeptides are rapidly cleared from cells via the ubiquitin-proteasome system (UPS). However, when the UPS is impaired, misfolded polypeptides form small cytoplasmic aggregates, which are sequestered into an aggresome and ultimately degraded by aggrephagy. Despite the relevance of the aggresome to neurodegenerative proteinopathies, the molecular mechanisms underlying aggresome formation remain unclear. Here we show that the CTIF-eEF1A1-DCTN1 (CED) complex functions in the surveillance of either pre-existing or newly synthesized polypeptides by linking two molecular events: selective recognition and aggresomal targeting of misfolded polypeptides. These events are accompanied by CTIF sequestration into the aggresome, preventing the additional synthesis of misfolded polypeptides from mRNAs bound by nuclear cap-binding complex. These events render cells more resistant to apoptosis induced by proteotoxic stresses. Collectively, our data provide compelling evidence for a previously unappreciated protein surveillance pathway and a regulatory gene expression network for coping with misfolded polypeptides.

Indexed as

ApoptosisProtein FoldingAutophagyBiological TransportCytoplasmDown-RegulationHEK293 CellsHeLa CellsHumansInclusion BodiesPeptide Elongation Factor 1PeptidesProteasome Endopeptidase ComplexProtein BindingProtein DenaturationProtein TransportEEF1A1 protein, humanPeptide Elongation Factor 1PeptidesProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID28589942
PMCPMC5467238

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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.