Evidence map›Paper›PMID 28727280›Full record

ArticleTraffic (Copenhagen, Denmark)2017

Two novel effectors of trafficking and maturation of the yeast plasma membrane H

Yosef Geva, Jonathan Crissman, Eric C Arakel, Natalia Gómez-Navarro, Silvia G Chuartzman, Kyle R Stahmer, Blanche Schwappach, Elizabeth A Miller, Maya Schuldiner

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2017. 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
0.5field-weighted citation impact, top 37% 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, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Protein quality control in the endoplasmic reticulum.Current opinion in cell biology · 2020
    Review
  7. Article
  8. Article
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

9 authors at 4 institutions in 4 countries.

Yosef GevaDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Jonathan CrissmanDepartment of Biological Sciences, Columbia University, New York, NY.
Eric C ArakelDepartment of Molecular Biology, Universitätsmedizin Göttingen, Göttingen, Germany.
Natalia Gómez-NavarroMRC Laboratory of Molecular Biology, Cell Biology Division, Cambridge, UK.
Silvia G ChuartzmanDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Kyle R StahmerDepartment of Biological Sciences, Columbia University, New York, NY.
Blanche SchwappachDepartment of Molecular Biology, Universitätsmedizin Göttingen, Göttingen, Germany.
Elizabeth A MillerDepartment of Biological Sciences, Columbia University, New York, NY.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-9947-115X
Weizmann Institute of Science · ILColumbia University · USMRC Laboratory of Molecular Biology · GBUniversitätsmedizin Göttingen · DE

Funding

CELLULAR AND MOLECULAR FOUNDATIONS OF BIOMEDICAL SCIENCET32GM008798 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PRYWES, RON M · 2001 to 2018
$6.3M
Molecular mechanisms of cargo capture into ER-derived transport vesiclesR01GM085089 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI BULINSKI, JEANNETTE CHLOE, MILLER, ELIZABETH A. · 2008 to 2016
$2.4M
Medical Research Council MC_UP_1201/10NIGMS NIH HHS R01 GM085089NIGMS NIH HHS T32 GM008798
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the entry site of proteins into the endomembrane system. Proteins exit the ER via coat protein II (COPII) vesicles in a selective manner, mediated either by direct interaction with the COPII coat or aided by cargo receptors. Despite the fundamental role of such receptors in protein sorting, only a few have been identified. To further define the machinery that packages secretory cargo and targets proteins from the ER to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized proteins that mediate the trafficking and maturation of Pma1, the essential yeast plasma membrane proton ATPase. Ydl121c (Exp1) is an ER protein that binds Pma1, is packaged into COPII vesicles, and whose deletion causes ER retention of Pma1. Ykl077w (Psg1) physically interacts with Exp1 and can be found in the Golgi and coat protein I (COPI) vesicles but does not directly bind Pma1. Loss of Psg1 causes enhanced degradation of Pma1 in the vacuole. Our findings suggest that Exp1 is a Pma1 cargo receptor and that Psg1 aids Pma1 maturation in the Golgi or affects its retrieval. More generally our work shows the utility of high content screens in the identification of novel trafficking components.

Indexed as

COP-Coated VesiclesGolgi ApparatusProtein BindingProtein TransportProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsPMA1 protein, S cerevisiaeProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsYdl121c protein, S cerevisiaeYkl077w protein, S cerevisiaeCOPICOPIIExp1Kex2Lst1Pma1Psg1Sec24Ydl121cYkl077w

Identifiers

PMID28727280
PMCPMC5607100
OpenAlexW2737553468

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.