Evidence map›Paper›PMID 23345439›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Arl1p regulates spatial membrane organization at the trans-Golgi network through interaction with Arf-GEF Gea2p and flippase Drs2p.

Pei-Chin Tsai, Jia-Wei Hsu, Ya-Wen Liu, Kuan-Yu Chen, Fang-Jen S Lee

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Knockout ofJournal of fungi (Basel, Switzerland) · 2026
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  15. Article
  16. Review
  17. Article
  18. Lipid flippases in polarized growth.Current genetics · 2021
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Pei-Chin TsaiInstitute of Molecular Medicine, College of Medicine, National Taiwan University, and Department of Medical Research, National Taiwan University Hospital, Taipei 100, Taiwan.
Jia-Wei Hsu
Ya-Wen Liu
Kuan-Yu Chen
Fang-Jen S Lee
National Taiwan University Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP ribosylation factors (Arfs) are the central regulators of vesicle trafficking from the Golgi complex. Activated Arfs facilitate vesicle formation through stimulating coat assembly, activating lipid-modifying enzymes and recruiting tethers and other effectors. Lipid translocases (flippases) have been implicated in vesicle formation through the generation of membrane curvature. Although there is no evidence that Arfs directly regulate flippase activity, an Arf-guanine-nucleotide-exchange factor (GEF) Gea2p has been shown to bind to and stimulate the activity of the flippase Drs2p. Here, we provide evidence for the interaction and activation of Drs2p by Arf-like protein Arl1p in yeast. We observed that Arl1p, Drs2p and Gea2p form a complex through direct interaction with each other, and each interaction is necessary for the stability of the complex and is indispensable for flippase activity. Furthermore, we show that this Arl1p-Drs2p-Gea2p complex is specifically required for recruiting golgin Imh1p to the Golgi. Our results demonstrate that activated Arl1p can promote the spatial modulation of membrane organization at the trans-Golgi network through interacting with the effectors Gea2p and Drs2p.

Indexed as

ADP-Ribosylation FactorsCalcium-Transporting ATPasesCell MembraneFluorescent Antibody Technique, IndirectGuanine Nucleotide Exchange FactorsHumansMembrane ProteinsPhosphatidylserinesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkTwo-Hybrid System TechniquesADP-ribosylation factor related proteinsADP-Ribosylation FactorsCalcium-Transporting ATPasesDRS2 protein, S cerevisiaeGEA2 protein, S cerevisiaeGuanine Nucleotide Exchange FactorsMembrane ProteinsPhosphatidylserinesSaccharomyces cerevisiae Proteins

Identifiers

PMID23345439
PMCPMC3581910
OpenAlexW2148994860

What OpenQuestion holds

Textmetadata
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.