Evidence map›Paper›PMID 22523562›Full record

ArticlePloS one2012

The interaction properties of the human Rab GTPase family--comparative analysis reveals determinants of molecular binding selectivity.

Matthias Stein, Manohar Pilli, Sabine Bernauer, Bianca H Habermann, Marino Zerial, Rebecca C Wade

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Elucidating the molecular interplay between LRRK2 and Rab GTPases.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Rab21 recruits EEA1 and competes with Rab5 for Rabex-5 activation.Frontiers in cell and developmental biology · 2025
    Article
  4. Review
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  9. Review
  10. Structure and Dynamics of Mono- vs. Doubly Lipidated Rab5 in Membranes.International journal of molecular sciences · 2019
    Article
  11. Article
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  13. Probing the druggability of membrane-bound Rab5 by molecular dynamics simulations.Journal of enzyme inhibition and medicinal chemistry · 2017
    Article
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  15. Article
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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 3 institutions in 1 country.

Matthias SteinMolecular and Cellular Modeling Group, Heidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany. matthias.stein@mpi-magdeburg.mpg.de
Manohar Pilli
Sabine Bernauer
Bianca H Habermann
Marino Zerial
Rebecca C Wade
Heidelberg Institute for Theoretical Studies · DEMax Planck Institute of Molecular Cell Biology and Genetics · DEMax Planck Institute for Biology of Ageing · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundRab GTPases constitute the largest subfamily of the Ras protein superfamily. Rab proteins regulate organelle biogenesis and transport, and display distinct binding preferences for effector and activator proteins, many of which have not been elucidated yet. The underlying molecular recognition motifs, binding partner preferences and selectivities are not well understood. METHODOLOGY/PRINCIPAL

findingsComparative analysis of the amino acid sequences and the three-dimensional electrostatic and hydrophobic molecular interaction fields of 62 human Rab proteins revealed a wide range of binding properties with large differences between some Rab proteins. This analysis assists the functional annotation of Rab proteins 12, 14, 26, 37 and 41 and provided an explanation for the shared function of Rab3 and 27. Rab7a and 7b have very different electrostatic potentials, indicating that they may bind to different effector proteins and thus, exert different functions. The subfamily V Rab GTPases which are associated with endosome differ subtly in the interaction properties of their switch regions, and this may explain exchange factor specificity and exchange kinetics. CONCLUSIONS/SIGNIFICANCE: We have analysed conservation of sequence and of molecular interaction fields to cluster and annotate the human Rab proteins. The analysis of three dimensional molecular interaction fields provides detailed insight that is not available from a sequence-based approach alone. Based on our results, we predict novel functions for some Rab proteins and provide insights into their divergent functions and the determinants of their binding partner selectivity.

Indexed as

Amino Acid SequenceGuanine Nucleotide Exchange FactorsHumansHydrophobic and Hydrophilic InteractionsMolecular Sequence DataProtein BindingProtein ConformationProtein Interaction Mappingrab GTP-Binding ProteinsSequence AlignmentStatic ElectricityGuanine Nucleotide Exchange Factorsrab GTP-Binding Proteins

Identifiers

PMID22523562
PMCPMC3327705
OpenAlexW2162492352

What OpenQuestion holds

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LicenceCC BY
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.