Evidence map›Paper›PMID 18418388›Full record

ArticleThe EMBO journal2008

Yeast and human Ysl2p/hMon2 interact with Gga adaptors and mediate their subcellular distribution.

Birgit Singer-Krüger, Maja Lasić, Anna-Maria Bürger, Angelika Hausser, Rüdiger Pipkorn, Yi Wang

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

15 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  6. Article
  7. Article
  8. Arl1 gets into the membrane remodeling business with a flippase and ArfGEF.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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 2 institutions in 1 country.

Birgit Singer-KrügerInstitute for Biochemistry, University of Stuttgart, Stuttgart, Germany. Singer-Krueger@ibc.uni-stuttgart.de
Maja Lasić
Anna-Maria Bürger
Angelika Hausser
Rüdiger Pipkorn
Yi Wang
University of Stuttgart · DEDKFZ-ZMBH Alliance · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Gga proteins represent a family of ubiquitously expressed clathrin adaptors engaged in vesicle budding at the tubular endosomal network/trans Golgi network. Their membrane recruitment is commonly thought to involve interactions with Arf and signals in cargo through the so-called VHS domain. For yeast Gga proteins, however, partners binding to its VHS domain have remained elusive and Gga localization does not absolutely depend on Arf. Here, we demonstrate that yeast Gga recruitment relies on a network of interactions between the scaffold Ysl2p/Mon2p, the small GTPase Arl1p, and the flippase Neo1p. Deletion of either YSL2 or ARL1 causes mislocalization of Gga2p, whereas a neo1-69 mutant accumulates Gga2p on aberrant structures. Remarkably, Ysl2p directly interacts with human and yeast Ggas through the VHS domain, and binding to Gga proteins is also found for the human Ysl2p orthologue hMon2. Thus, Ysl2p represents an essential, evolutionarily conserved member of a network controlling direct binding and membrane docking of Ggas. Because activated Arl1p is part of the network that binds Gga2p, Arf and Arf-like GTPases may interact in a regulatory cascade.

Indexed as

Adaptor Proteins, Vesicular TransportAdenosine TriphosphatasesADP-Ribosylation FactorsCell LineEndosomesGene DeletionHumansMembrane Transport ProteinsMonomeric GTP-Binding ProteinsPhospholipid Transfer ProteinsProtein Structure, TertiaryProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAdaptor Proteins, Vesicular TransportAdenosine TriphosphatasesADP-Ribosylation FactorsARL1 protein, S cerevisiaeGga2 protein, S cerevisiaeGGA adaptor proteinsMembrane Transport ProteinsMON2 protein, humanMON2 protein, S cerevisiaeMonomeric GTP-Binding ProteinsNEO1 protein, S cerevisiaePhospholipid Transfer ProteinsProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID18418388
PMCPMC2396392
OpenAlexW2142206989

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.