Evidence map›Paper›PMID 27552051›Full record

ArticleeLife2016

bMERB domains are bivalent Rab8 family effectors evolved by gene duplication.

Amrita Rai, Anastasia Oprisko, Jeremy Campos, Yangxue Fu, Timon Friese, Aymelt Itzen, Roger S Goody, Emerich Mihai Gazdag, Matthias P Müller

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 77 citations in OpenAlex.

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  8. HIV-1 budding requires cortical actin disassembly by the oxidoreductase MICAL1.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  9. Structural basis of MICAL autoinhibition.Nature communications · 2024
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  13. EHBP1 Is Critically Involved in the Dendritic Arbor Formation and Is Coupled to Factors Promoting Actin Filament Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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  18. Host Cell Signatures of the Envelopment Site within Beta-Herpes Virions.International journal of molecular sciences · 2022
    Review
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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

9 authors at 2 institutions in 1 country.

Amrita RaiDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Anastasia OpriskoDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Jeremy CamposDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Yangxue FuDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Timon FrieseDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Aymelt ItzenCenter for Integrated Protein Science Munich (CIPSM), Department of Chemistry, Technische Universität München, Garching, Germany.
Roger S GoodyDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-0772-0444
Emerich Mihai GazdagDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Matthias P MüllerDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-1529-8933
Max Planck Institute of Molecular Physiology · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study, we have thoroughly characterized a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterize a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.

Indexed as

Evolution, MolecularGene DuplicationAdaptor Proteins, Signal TransducingCalponinsCarrier ProteinsCytoskeletal ProteinsLIM Domain ProteinsMicrofilament ProteinsMixed Function OxygenasesProtein Domainsrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingCalponinsCarrier ProteinsCytoskeletal ProteinsEHBP1 protein, humanLIM Domain ProteinsMICAL1 protein, humanMicrofilament ProteinsMixed Function OxygenasesRAB8A protein, humanrab GTP-Binding ProteinsbiochemistrybiophysicsEHBPhumanMicalRab effectorsstructural biology

Identifiers

PMID27552051
PMCPMC5026484
OpenAlexW2518491015

What OpenQuestion holds

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Registered trials

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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.