Evidence map›Paper›PMID 26771486›Full record

ArticleCell2016

The Protease Ste24 Clears Clogged Translocons.

Tslil Ast, Susan Michaelis, Maya Schuldiner

Abstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing 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

74 citing papers in PubMed.

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14 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

3 authors.

Tslil AstDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Susan MichaelisDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address: maya.schuldiner@weizmann.ac.il.

Funding

The integral membrane protease ZMPSTE24, lamin A processing, and progeriaR01GM041223 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MICHAELIS, SUSAN D. · 1989 to 2017
$5.0M
NIGMS NIH HHS R01 GM041223NIGMS NIH HHS R01GM041223
6 · The paper itself

Abstract

Translocation into the endoplasmic reticulum (ER) is the first step in the biogenesis of thousands of eukaryotic endomembrane proteins. Although functional ER translocation has been avidly studied, little is known about the quality control mechanisms that resolve faulty translocational states. One such faulty state is translocon clogging, in which the substrate fails to properly translocate and obstructs the translocon pore. To shed light on the machinery required to resolve clogging, we carried out a systematic screen in Saccharomyces cerevisiae that highlighted a role for the ER metalloprotease Ste24. We could demonstrate that Ste24 approaches the translocon upon clogging, and it interacts with and generates cleavage fragments of the clogged protein. Importantly, these functions are conserved in the human homolog, ZMPSTE24, although disease-associated mutant forms of ZMPSTE24 fail to clear the translocon. These results shed light on a new and critical task of Ste24, which safeguards the essential process of translocation.

Indexed as

Protein TransportEndoplasmic ReticulumHumansMembrane ProteinsMetalloendopeptidasesProtein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal Recognition ParticleMembrane ProteinsMetalloendopeptidasesSaccharomyces cerevisiae ProteinsSignal Recognition ParticleSTE24 protein, S cerevisiaeZMPSTE24 protein, human

Identifiers

PMID26771486
PMCPMC4715265

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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.