Evidence map›Paper›PMID 36651113›Full record

ArticleJournal of cell science2023

The C-terminus of the cargo receptor Erv14 affects COPII vesicle formation and cargo delivery.

Daniel Lagunas-Gomez, Carolina Yañez-Dominguez, Guadalupe Zavala-Padilla, Charles Barlowe, Omar Pantoja

Open access · hybridFull text read
In one paragraph

Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Trafficking of the human NaProtein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. 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

5 authors at 3 institutions in 2 countries.

Daniel Lagunas-GomezCentro de Investigación en Dinámica Celular, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca, Morelos 62210, Mexico.
Carolina Yañez-DominguezInstituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001, Cuernavaca, Morelos 62210, México.
Guadalupe Zavala-PadillaInstituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001, Cuernavaca, Morelos 62210, México.
Charles BarloweDepartment of Biochemistry, Geisel School of Medicine, Dartmouth College, Hanover, NH 03755-3844, USA.
Omar PantojaInstituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001, Cuernavaca, Morelos 62210, México.ORCID 0000-0002-6538-9059
Universidad Nacional Autónoma de México · MXDartmouth College · USUniversidad Autónoma del Estado de Morelos · MX

Funding

Mechanisms of COPII-dependent TransportR01GM052549 · NIGMS · DARTMOUTH COLLEGE · PI BARLOWE, CHARLES K · 1995 to 2024
$7.2M
NIGMS NIH HHS R01 GM052549
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little is known about how post-translational modification events regulate packaging of cargo into COPII vesicles. The Saccharomyces cerevisiae protein Erv14, also known as cornichon, belongs to a conserved family of cargo receptors required for the selection and ER export of transmembrane proteins. In this work, we show the importance of a phosphorylation consensus site (S134) at the C-terminus of Erv14. Mimicking phosphorylation of S134 (S134D) prevents the incorporation of Erv14 into COPII vesicles, delays cell growth, exacerbates growth of sec mutants, modifies ER structure and affects localization of several plasma membrane transporters. In contrast, the dephosphorylated mimic (S134A) had less deleterious effects, but still modifies ER structure and slows cell growth. Our results suggest that a possible cycle of phosphorylation and dephosphorylation is important for the correct functioning of Erv14.

Indexed as

Saccharomyces cerevisiae ProteinsBiological TransportCarrier ProteinsCOP-Coated VesiclesMembrane ProteinsMembrane Transport ProteinsProtein TransportCarrier ProteinsMembrane ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae ProteinsCOPII vesiclesCornichonErv14Membrane traffickingPhosphorylation

Identifiers

PMID36651113
PMCPMC10022740
OpenAlexW4317207066

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read127
identifiers read1
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.