Evidence map›Paper›PMID 23898197›Full record

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

Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopy.

Konstantin Gavriljuk, Aymelt Itzen, Roger S Goody, Klaus Gerwert, Carsten Kötting

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. GDI2 protein: research progress and its mechanisms in diseases.Frontiers in cell and developmental biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Crystal structure of the GDP-bound GTPase domain of Rab5a from Leishmania donovani.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  9. Review
  10. Article
  11. Adipose tissue depot-specific intracellular and extracellular cues contributing to insulin resistance in obese individuals.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  12. Stochastic activation and bistability in a Rab GTPase regulatory network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Structure and function of Fic proteins.Nature reviews. Microbiology · 2015
    Review
  17. Article
  18. Rab proteins and the compartmentalization of the endosomal system.Cold Spring Harbor perspectives in biology · 2014
    Review
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.

Konstantin GavriljukDepartment of Biophysics, Ruhr-University Bochum, 44801 Bochum, Germany.
Aymelt Itzen
Roger S Goody
Klaus Gerwert
Carsten Kötting
Ruhr University Bochum · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane trafficking is regulated by small Ras-like GDP/GTP binding proteins of the Rab subfamily (Rab GTPases) that cycle between membranes and cytosol depending on their nucleotide state. The GDP dissociation inhibitor (GDI) solubilizes prenylated Rab GTPases from and shuttles them between membranes in the form of a soluble cytosolic complex. We use attenuated total reflection-Fourier transform infrared spectroscopy to directly observe extraction of Rab GTPases from model membranes by GDI. In their native form, most Rab GTPases are doubly geranylgeranylated at the C terminus to achieve localization to the membrane. We find that monogeranylgeranylated Rab35 and Rab1b reversibly bind to a negatively charged model membrane. Correct folding and GTPase activity of the membrane-bound protein can be evaluated. The dissociation kinetics depends on the C-terminal sequence and charge of the GTPases. The attenuated total reflection experiments show that GDI genuinely accelerates the intrinsic Rab membrane dissociation. The extraction process is characterized and occurs in a nucleotide-dependent manner. Furthermore, we find that phosphocholination of Rab35, which is catalyzed by the Legionella pneumophila protein AnkX, interferes with the ability of GDI to extract Rab35 from the membrane. The attenuated total reflection-Fourier transform infrared spectroscopy approach enables label-free investigation of the interaction between GDI and Rab GTPases in a membrane environment. Thereby, GDI is revealed to actively extract monogeranylgeranylated membrane-bound Rab GTPases and, thus, is not merely a solubilization factor.

Indexed as

AnimalsCattleGuanine Nucleotide Dissociation InhibitorsKineticsLegionella pneumophilaMembranesPhosphorylcholinePrenylationrab GTP-Binding ProteinsSaccharomyces cerevisiaeSpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredTransport VesiclesGDP dissociation inhibitor 1Guanine Nucleotide Dissociation InhibitorsPhosphorylcholinerab GTP-Binding Proteinsgeranylgeranyllipid bilayersRab recyclingvesicle spreading

Identifiers

PMID23898197
PMCPMC3746908
OpenAlexW2099564767

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.