Evidence map›Paper›PMID 29887313›Full record

ArticleCurrent biology : CB2018

Lysophospholipids Facilitate COPII Vesicle Formation.

Alejandro Melero, Nicolas Chiaruttini, Takefumi Karashima, Isabelle Riezman, Kouichi Funato, Charles Barlowe, Howard Riezman, Aurélien Roux

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 56 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 3 countries.

Alejandro MeleroDepartment of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland.
Nicolas ChiaruttiniDepartment of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
Takefumi KarashimaDepartment of Bioresource Science and Technology, Hiroshima University, Hiroshima 739-8528, Japan.
Isabelle RiezmanDepartment of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
Kouichi FunatoDepartment of Bioresource Science and Technology, Hiroshima University, Hiroshima 739-8528, Japan.
Charles BarloweDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755-3844, USA.
Howard RiezmanDepartment of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland. Electronic address: howard.riezman@unige.ch.
Aurélien RouxDepartment of Biochemistry, University of Geneva, 1211 Geneva, Switzerland; Swiss National Centre for Competence in Research in Chemical Biology, 1211 Geneva, Switzerland. Electronic address: aurelien.roux@unige.ch.
University of Geneva · CHFORS – Swiss Centre of Expertise in the Social Sciences · CHHiroshima University · JPDartmouth College · US

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

Coat protein complex II (COPII) proteins form vesicles from the endoplasmic reticulum to export cargo molecules to the Golgi apparatus. Among the many proteins involved in this process, Sec12 is a key regulator, functioning as the guanosine diphosphate (GDP) exchange factor for Sar1p, the small guanosine triphosphatase (GTPase) that initiates COPII assembly. Here we show that overexpression of phospholipase B3 in the thermosensitive sec12-4 mutant partially restores growth and protein transport at non-permissive temperatures. Lipidomics analyses of these cells show a higher content of lysophosphatidylinositol (lysoPI), consistent with the lipid specificity of PLB3. Furthermore, we show that lysoPI is specifically enriched in COPII vesicles isolated from in vitro budding assays. As these results suggested that lysophospholipids could facilitate budding under conditions of defective COPII coat dynamics, we reconstituted COPII binding onto giant liposomes with purified proteins and showed that lysoPI decreases membrane rigidity and enhances COPII recruitment to liposomes. Our results support a mechanical facilitation of COPII budding by lysophospholipids.

Indexed as

COP-Coated VesiclesLysophospholipidsMicrosomesSaccharomyces cerevisiaelysophosphatidylinositolLysophospholipidsbudding assaysCOPIIlysolipidsmembrane curvaturemembrane rigidityphospholipasevesicular transport

Identifiers

PMID29887313
PMCPMC6013297
OpenAlexW2807458786

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.