Evidence map›Paper›PMID 26650540›Full record

ArticleTraffic (Copenhagen, Denmark)2016

Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins.

Neil G Margulis, Joshua D Wilson, Christine M Bentivoglio, Nripesh Dhungel, Aaron D Gitler, Charles Barlowe

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Neil G MargulisDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.
Joshua D WilsonDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.
Christine M BentivoglioDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.
Nripesh DhungelDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Aaron D GitlerDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Charles BarloweDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.
Dartmouth College · USSinger (United States) · USStanford University · US

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
A Stanford - SJSU Postdoctoral Training Program to Enhance URM TeachingK12GM088033 · NIGMS · STANFORD UNIVERSITY · PI BOOTHROYD, JOHN C · 2010 to 2016
$4.1M
Molecular Basis of TDP-43 Proteinopathies: Disease Models and MechanismsR01NS065317 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI GITLER, AARON D. · 2009 to 2016
$2.7M
NIGMS NIH HHS K12 GM088033NIGMS NIH HHS K12-GM088033NIGMS NIH HHS R01 GM052549NIGMS NIH HHS R37 GM052549NIGMS NIH HHS R37GM052549NINDS NIH HHS R01 NS065317NINDS NIH HHS R01NS065317
6 · The paper itself

Abstract

Coat protein complex II (COPII) vesicle formation at the endoplasmic reticulum (ER) transports nascent secretory proteins forward to the Golgi complex. To further define the machinery that packages secretory cargo and targets vesicles to Golgi membranes, we performed a comprehensive proteomic analysis of purified COPII vesicles. In addition to previously known proteins, we identified new vesicle proteins including Coy1, Sly41 and Ssp120, which were efficiently packaged into COPII vesicles for trafficking between the ER and Golgi compartments. Further characterization of the putative calcium-binding Ssp120 protein revealed a tight association with Emp47 and in emp47Δ cells Ssp120 was mislocalized and secreted. Genetic analyses demonstrated that EMP47 and SSP120 display identical synthetic positive interactions with IRE1 and synthetic negative interactions with genes involved in cell wall assembly. Our findings support a model in which the Emp47-Ssp120 complex functions in transport of plasma membrane glycoproteins through the early secretory pathway.

Indexed as

Secretory PathwayCOP-Coated VesiclesGlycoproteinsMembrane GlycoproteinsProtein BindingProtein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsEMP47 protein, S cerevisiaeGlycoproteinsIRE1 protein, S cerevisiaeMembrane GlycoproteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSSP120 protein, S cerevisiaeVesicular Transport Proteinscargo receptorsCOPII coatendoplasmic reticulumGolgiprotein secretionprotein traffickingvesicle budding

Identifiers

PMID26650540
PMCPMC4767645
OpenAlexW2194991829

What OpenQuestion holds

Textmetadata
LicenceTDM
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.