Evidence map›Paper›PMID 25801167›Full record

ArticleMolecular cell2015

Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.

Brian J Conti, Prasanna K Devaraneni, Zhongying Yang, Larry L David, William R Skach

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

64 citing papers in PubMed, 117 citations in OpenAlex.

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4 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

5 authors at 1 institution in 1 country.

Brian J ContiDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA. Electronic address: contib@ohsu.edu.
Prasanna K DevaraneniDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA.
Zhongying YangDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA.
Larry L DavidDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA.
William R SkachDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA; Cystic Fibrosis Foundation Therapeutics, Inc., Bethesda, MD 20814, USA.
Oregon Health & Science University · US

Funding

Understanding the origins of rapid recurrence of pancreatic cancer after resectionP30CA069533 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI Luiz Eduardo Bertassoni · 1997 to 2026
$60.5M
Proteomics CoreP30EY010572 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI TED S ACOTT · 1995 to 2026
$19.4M
Multidisciplinary Research Training in Pulmonary MedicineT32HL083808 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LEWINSOHN, DAVID M., SLATORE, CHRISTOPHER G. · 2008 to 2025
$5.3M
MECHANISMS OF POLYTOPIC PROTEIN BIOGENESIS IN THE ERR01GM053457 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI SKACH, WILLIAM R · 1996 to 2013
$3.5M
BIOGENESIS AND MOLECULAR PATHOGENESIS OF CFTRR01DK051818 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI SKACH, WILLIAM R · 1997 to 2012
$2.9M
LTQ Orbitrap VelosS10OD012246 · OD · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAVID, LARRY L · 2012 to 2012
$854k
Mechanisms of Sec61-Mediated Polytopic Protein Integration into the ERF32GM083568 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI CONTI, BRIAN J · 2008 to 2009
$101k
NCI NIH HHS P30 CA069533NCI NIH HHS P30CA069533NEI NIH HHS P30 EY010572NEI NIH HHS P30EY010572NHLBI NIH HHS T32 HL083808NIDDK NIH HHS DK51818NIDDK NIH HHS R01 DK051818NIGMS NIH HHS F32 GM083568NIGMS NIH HHS GM53457NIGMS NIH HHS R01 GM053457NIH HHS S10 OD012246NIH HHS S10OD012246
6 · The paper itself

Abstract

The ER Sec61 translocon is a large macromolecular machine responsible for partitioning secretory and membrane polypeptides into the lumen, cytosol, and lipid bilayer. Because the Sec61 protein-conducting channel has been isolated in multiple membrane-derived complexes, we determined how the nascent polypeptide modulates translocon component associations during defined cotranslational translocation events. The model substrate preprolactin (pPL) was isolated principally with Sec61αβγ upon membrane targeting, whereas higher-order complexes containing OST, TRAP, and TRAM were stabilized following substrate translocation. Blocking pPL translocation by passenger domain folding favored stabilization of an alternate complex that contained Sec61, Sec62, and Sec63. Moreover, Sec62/63 stabilization within the translocon occurred for native endogenous substrates, such as the prion protein, and correlated with a delay in translocation initiation. These data show that cotranslational translocon contacts are ultimately controlled by the engaged nascent chain and the resultant substrate-driven translocation events.

Indexed as

AnimalsEndoplasmic ReticulumEnzyme StabilityMammalsMembrane ProteinsPrionsProlactinProtein PrecursorsProtein TransportSubstrate SpecificityMembrane ProteinspreprolactinPrionsProlactinProtein Precursors

Identifiers

PMID25801167
PMCPMC4402133
OpenAlexW1991344063

What OpenQuestion holds

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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.