Evidence map›Paper›PMID 24866125›Full record

ArticleMolecular & cellular proteomics : MCP2014

Rapid mapping of interactions between Human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy.

Emma Sierecki, Loes M Stevers, Nichole Giles, Mark E Polinkovsky, Mehdi Moustaqil, Sergey Mureev, Wayne A Johnston, Mareike Dahmer-Heath, Dubravka Skalamera, Thomas J Gonda and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

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  13. Lmo1656 is a secreted virulence factor ofThe Journal of biological chemistry · 2018
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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

14 authors at 2 institutions in 1 country.

Emma SiereckiFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Loes M SteversFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Nichole GilesFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Mark E PolinkovskyFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Mehdi MoustaqilFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Sergey MureevFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Wayne A JohnstonFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Mareike Dahmer-Heath§University of Queensland, Diamantina Institute, Translational Research Institute, Brisbane, Australia;
Dubravka Skalamera§University of Queensland, Diamantina Institute, Translational Research Institute, Brisbane, Australia;
Thomas J Gonda¶School of Pharmacy, The University of Queensland, Brisbane, Australia.
Brian Gabrielli§University of Queensland, Diamantina Institute, Translational Research Institute, Brisbane, Australia;
Brett M CollinsFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
Kirill AlexandrovFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia; y.gambin@uq.edu.au k.alexandrov@uq.edu.au.
Yann GambinFrom the ‡Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072 Australia;
University of Queensland · AUTranslational Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein dimerization and oligomerization is commonly used by nature to increase the structural and functional complexity of proteins. Regulated protein assembly is essential to transfer information in signaling, transcriptional, and membrane trafficking events. Here we show that a combination of cell-free protein expression, a proximity based interaction assay (AlphaScreen), and single-molecule fluorescence allow rapid mapping of homo- and hetero-oligomerization of proteins. We have applied this approach to the family of BAR domain-containing sorting nexin (SNX-BAR) proteins, which are essential regulators of membrane trafficking and remodeling in all eukaryotes. Dimerization of BAR domains is essential for creating a concave structure capable of sensing and inducing membrane curvature. We have systematically mapped 144 pairwise interactions between the human SNX-BAR proteins and generated an interaction matrix of preferred dimerization partners for each family member. We find that while nine SNX-BAR proteins are able to form homo-dimers, several including the retromer-associated SNX1, SNX2, and SNX5 require heteromeric interactions for dimerization. SNX2, SNX4, SNX6, and SNX8 show a promiscuous ability to bind other SNX-BAR proteins and we also observe a novel interaction with the SNX3 protein which lacks the BAR domain structure.

Indexed as

DimerizationHumansProtein Interaction MappingProtein Structure, TertiarySorting NexinsSpectrometry, FluorescenceSorting Nexins

Identifiers

PMID24866125
PMCPMC4159646
OpenAlexW2159268987

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.