Evidence map›Paper›PMID 24019533›Full record

ArticleThe Journal of cell biology2013

Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport.

Peng Xu, Ryan D Baldridge, Richard J Chi, Christopher G Burd, Todd R Graham

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
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  7. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
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18 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Peng XuDepartment of Biological Sciences, Vanderbilt University, Nashville, TN 37235.
Ryan D Baldridge
Richard J Chi
Christopher G Burd
Todd R Graham
Vanderbilt University · USYale University · US

Funding

TRAFFICKING BY FYVE DOMAIN EFFECTORS OF PI3 KINASER01GM061221 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2000 to 2016
$5.2M
Drs2p Function in Clathrin-coated Vesicle BuddingR01GM062367 · NIGMS · VANDERBILT UNIVERSITY · PI GRAHAM, TODD R · 2001 to 2013
$3.4M
PtdIns 4-Kinase Regulation of Protein Sorting in the Golgi ApparatusR01GM095766 · NIGMS · YALE UNIVERSITY · PI BURD, CHRISTOPHER G · 2011 to 2021
$2.9M
P4-ATPase mechanism of phospholipid translocationR01GM107978 · NIGMS · VANDERBILT UNIVERSITY · PI GRAHAM, TODD R · 2013 to 2021
$2.5M
NIGMS NIH HHS R01 GM061221NIGMS NIH HHS R01 GM062367NIGMS NIH HHS R01GM062367NIGMS NIH HHS R01 GM095766NIGMS NIH HHS R01 GM107978
6 · The paper itself

Abstract

Vesicle-mediated protein transport between organelles of the secretory and endocytic pathways is strongly influenced by the composition and organization of membrane lipids. In budding yeast, protein transport between the trans-Golgi network (TGN) and early endosome (EE) requires Drs2, a phospholipid translocase in the type IV P-type ATPase family. However, downstream effectors of Drs2 and specific phospholipid substrate requirements for protein transport in this pathway are unknown. Here, we show that the Arf GTPase-activating protein (ArfGAP) Gcs1 is a Drs2 effector that requires a variant of the ArfGAP lipid packing sensor (+ALPS) motif for localization to TGN/EE membranes. Drs2 increases membrane curvature and anionic phospholipid composition of the cytosolic leaflet, both of which are sensed by the +ALPS motif. Using mutant forms of Drs2 and the related protein Dnf1, which alter their ability to recognize phosphatidylserine, we show that translocation of this substrate to the cytosolic leaflet is essential for +ALPS binding and vesicular transport between the EE and the TGN.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceATP-Binding Cassette TransportersBlotting, WesternCalcium-Transporting ATPasesCell MembraneDNA-Binding ProteinsEndosomesGTPase-Activating ProteinsImmunoprecipitationMembrane LipidsModels, MolecularMolecular Sequence DataPhosphatidylserinesSaccharomyces cerevisiaeAdenosine TriphosphatasesATP-Binding Cassette TransportersCalcium-Transporting ATPasesDNA-Binding ProteinsDnf1 protein, S cerevisiaeDRS2 protein, S cerevisiaeGCS1 protein, S cerevisiaeGTPase-Activating ProteinsMembrane LipidsPhosphatidylserinesSaccharomyces cerevisiae Proteins

Identifiers

PMID24019533
PMCPMC3776346
OpenAlexW2104891965

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.