Evidence map›Paper›PMID 26538028›Full record

ArticleMolecular biology of the cell2016

Auxilin facilitates membrane traffic in the early secretory pathway.

Jingzhen Ding, Verónica A Segarra, Shuliang Chen, Huaqing Cai, Sandra K Lemmon, Susan Ferro-Novick

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-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

14 citing papers in PubMed, 18 citations in OpenAlex.

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  14. Clathrin in plant defense signaling and execution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

6 authors at 3 institutions in 2 countries.

Jingzhen DingDepartment of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0668.
Verónica A SegarraDepartment of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33136.
Shuliang ChenDepartment of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0668.
Huaqing CaiState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Sandra K LemmonDepartment of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33136 sfnovick@ucsd.edu slemmon@med.miami.edu.
Susan Ferro-NovickDepartment of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0668 sfnovick@ucsd.edu slemmon@med.miami.edu.
Howard Hughes Medical Institute · USUniversity of Miami · USChinese Academy of Sciences · CN

Funding

SUPPRESSORS OF CLATHRIN DEFICIENCY IN YEASTR01GM055796 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LEMMON, SANDRA K. · 1998 to 2015
$4.7M
TRAINING PROGRAMS IN CARDIOVASCULAR PHARMACOLOGYT32HL007188 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SZCZESNA-CORDARY, DANUTA · 1985 to 2011
$3.8M
The role of a CK1 kinase in membrane trafficR01GM114111 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FERRO-NOVICK, SUSAN · 2015 to 2018
$1.5M
NHLBI NIH HHS T32 HL007188NHLBI NIH HHS T32-HL07188NIGMS NIH HHS R01 GM 055796NIGMS NIH HHS R01 GM055796NIGMS NIH HHS R01 GM114111
6 · The paper itself

Abstract

Coat protein complexes contain an inner shell that sorts cargo and an outer shell that helps deform the membrane to give the vesicle its shape. There are three major types of coated vesicles in the cell: COPII, COPI, and clathrin. The COPII coat complex facilitates vesicle budding from the endoplasmic reticulum (ER), while the COPI coat complex performs an analogous function in the Golgi. Clathrin-coated vesicles mediate traffic from the cell surface and between the trans-Golgi and endosome. While the assembly and structure of these coat complexes has been extensively studied, the disassembly of COPII and COPI coats from membranes is less well understood. We describe a proteomic and genetic approach that connects the J-domain chaperone auxilin, which uncoats clathrin-coated vesicles, to COPII and COPI coat complexes. Consistent with a functional role for auxilin in the early secretory pathway, auxilin binds to COPII and COPI coat subunits. Furthermore, ER-Golgi and intra-Golgi traffic is delayed at 15°C in swa2Δ mutant cells, which lack auxilin. In the case of COPII vesicles, we link this delay to a defect in vesicle fusion. We propose that auxilin acts as a chaperone and/or uncoating factor for transport vesicles that act in the early secretory pathway.

Indexed as

AuxilinsClathrinClathrin-Coated VesiclesCOP-Coated VesiclesEndoplasmic ReticulumGolgi ApparatusMembrane ProteinsProtein TransportProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory PathwayVesicular Transport ProteinsAuxilinsClathrinMembrane ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID26538028
PMCPMC4694752
OpenAlexW2305596469

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.