Evidence map›Paper›PMID 16395334›Full record

ArticleThe EMBO journal2006

Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling.

Olena Pylypenko, Alexey Rak, Thomas Durek, Susanna Kushnir, Beatrice E Dursina, Nicolas H Thomae, Alexandru T Constantinescu, Luc Brunsveld, Anja Watzke, Herbert Waldmann and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proteolysis of Rab32 byiScience · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Biotechnological Applications of Protein Splicing.Current protein & peptide science · 2019
    Review
  18. Review
  19. Review
  20. 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

12 authors at 2 institutions in 2 countries.

Olena PylypenkoMax-Planck-Institute for Molecular Physiology, Dortmund, Germany.
Alexey Rak
Thomas Durek
Susanna Kushnir
Beatrice E Dursina
Nicolas H Thomae
Alexandru T Constantinescu
Luc Brunsveld
Anja Watzke
Herbert Waldmann
Roger S Goody
Kirill Alexandrov
Max Planck Society · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cells Rab/Ypt GTPases represent a family of key membrane traffic controllers that associate with their targeted membranes via C-terminally conjugated geranylgeranyl groups. GDP dissociation inhibitor (GDI) is a general and essential regulator of Rab recycling that extracts prenylated Rab proteins from membranes at the end of their cycle of activity and facilitates their delivery to the donor membranes. Here, we present the structure of a complex between GDI and a doubly prenylated Rab protein. We show that one geranylgeranyl residue is deeply buried in a hydrophobic pocket formed by domain II of GDI, whereas the other lipid is more exposed to solvent and is skewed across several atoms of the first moiety. Based on structural information and biophysical measurements, we propose mechanistic and thermodynamic models for GDI and Rab escort protein-mediated interaction of RabGTPase with intracellular membranes.

Indexed as

Adaptor Proteins, Signal TransducingBinding SitesCrystallography, X-RayGuanine Nucleotide Dissociation InhibitorsIntracellular MembranesLipidsProtein Conformationrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSolubilityThermodynamicsAdaptor Proteins, Signal TransducingGuanine Nucleotide Dissociation InhibitorsLipidsMRS6 protein, S cerevisiaerab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSEC4 protein, S cerevisiae

Identifiers

PMID16395334
PMCPMC1356364
OpenAlexW2145129663

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.