Evidence map›Paper›PMID 30067224›Full record

ArticleeLife2018

Structural insights into the architecture and membrane interactions of the conserved COMMD proteins.

Michael D Healy, Manuela K Hospenthal, Ryan J Hall, Mintu Chandra, Molly Chilton, Vikas Tillu, Kai-En Chen, Dion J Celligoi, Fiona J McDonald, Peter J Cullen and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. 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
1.4field-weighted citation impact, top 21% 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, 49 citations in OpenAlex.

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  15. Structural Organization of the Retriever-CCC Endosomal Recycling Complex.bioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Article
  18. COMMD3 loss drives invasive breast cancer growth by modulating copper homeostasis.Journal of experimental & clinical cancer research : CR · 2023
    Article
  19. Review
  20. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    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

13 authors at 4 institutions in 3 countries.

Michael D HealyInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0003-2924-9179
Manuela K HospenthalSchool of Biological Sciences, The University of Auckland, Auckland, New Zealand.
Ryan J HallInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0002-8543-0370
Mintu ChandraInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.
Molly ChiltonSchool of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, United Kingdom.ORCID http://orcid.org/0000-0003-2238-9822
Vikas TilluInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0002-1034-9543
Kai-En ChenInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0003-1106-1629
Dion J CelligoiSchool of Biological Sciences, The University of Auckland, Auckland, New Zealand.
Fiona J McDonaldDepartment of Physiology, University of Otago, Dunedin, New Zealand.
Peter J CullenSchool of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol, United Kingdom.
J Shaun LottSchool of Biological Sciences, The University of Auckland, Auckland, New Zealand.ORCID https://orcid.org/0000-0003-3660-452X
Brett M CollinsInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0002-6070-3774
Rajesh GhaiInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, Australia.ORCID http://orcid.org/0000-0002-0919-0934
The University of Queensland · AUUniversity of Auckland · NZUniversity of Bristol · GBUniversity of Otago · NZ

Funding

Australian Research Council DP160101743Medical Research Council MR/K018299/1Medical Research Council MR/P018807/1National Health and Medical Research Council 1097185National Health and Medical Research Council APP1058734National Health and Medical Research Council APP1061574Royal Society of New Zealand Marsden fund: UOO-04-09University of Queensland Early career researcher grant: 2016003796Wellcome 89928Wellcome TrustWellcome Trust 089928Wellcome Trust 104568
6 · The paper itself

Abstract

The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediates the transport of several transmembrane cargos. How these complexes are formed however is completely unknown. Here, we have systematically characterised the interactions between human COMMD proteins, and determined structures of COMMD proteins using X-ray crystallography and X-ray scattering to provide insights into the underlying mechanisms of homo- and heteromeric assembly. All COMMD proteins possess an α-helical N-terminal domain, and a highly conserved C-terminal domain that forms a tightly interlocked dimeric structure responsible for COMMD-COMMD interactions. The COMM domains also bind directly to components of CCC and mediate non-specific membrane association. Overall these studies show that COMMD proteins function as obligatory dimers with conserved domain architectures.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceCrystallography, X-RayEndosomesHumansIntracellular MembranesMembrane Transport ProteinsMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Conformation, alpha-HelicalProtein DomainsProtein Interaction MappingSequence AlignmentSignal TransductionTranscription, GeneticAdaptor Proteins, Signal TransducingCOMMD9 protein, humanMembrane Transport ProteinsMultiprotein ComplexesCCC complexcell biologyCommander complexcopper metabolism Murr1 domain containing (COMMD)endosomehumanmembrane traffickingmolecular biophysicsretrieverstructural biology

Identifiers

PMID30067224
PMCPMC6089597
OpenAlexW2886591234

What OpenQuestion holds

Textmetadata
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.