Evidence map›Paper›PMID 25882846›Full record

ArticleThe Journal of biological chemistry2015

Structure and Membrane Binding Properties of the Endosomal Tetratricopeptide Repeat (TPR) Domain-containing Sorting Nexins SNX20 and SNX21.

Thomas Clairfeuille, Suzanne J Norwood, Xiaying Qi, Rohan D Teasdale, Brett M Collins

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

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  10. Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021
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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

5 authors at 1 institution in 1 country.

Thomas ClairfeuilleFrom the Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Suzanne J NorwoodFrom the Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Xiaying QiFrom the Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Rohan D TeasdaleFrom the Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia.
Brett M CollinsFrom the Institute for Molecular Bioscience, University of Queensland, St. Lucia, Queensland 4072, Australia b.collins@imb.uq.edu.au.
University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sorting nexins (SNX) orchestrate membrane trafficking and signaling events required for the proper distribution of proteins within the endosomal network. Their phox homology (PX) domain acts as a phosphoinositide (PI) recognition module that targets them to specific endocytic membrane domains. The modularity of SNX proteins confers a wide variety of functions from signaling to membrane deformation and cargo binding, and many SNXs are crucial modulators of endosome dynamics and are involved in a myriad of physiological and pathological processes such as neurodegenerative diseases, cancer, and inflammation. Here, we have studied the poorly characterized SNX20 and its paralogue SNX21, which contain an N-terminal PX domain and a C-terminal PX-associated B (PXB) domain of unknown function. The two proteins share similar PI-binding properties and are recruited to early endosomal compartments by their PX domain. The crystal structure of the SNX21 PXB domain reveals a tetratricopeptide repeat (TPR)-fold, a module that typically binds short peptide motifs, with three TPR α-helical repeats. However, the C-terminal capping helix adopts a highly unusual and potentially self-inhibitory topology. SAXS solution structures of SNX20 and SNX21 show that these proteins adopt a compact globular architecture, and membrane interaction analyses indicate the presence of overlapping PI-binding sites that may regulate their intracellular localization. This study provides the first structural analysis of this poorly characterized subfamily of SNX proteins, highlighting a likely role as endosome-associated scaffolds.

Indexed as

Amino Acid SequenceAnimalsBinding SitesConserved SequenceCrystallography, X-RayEndosomesMiceModels, MolecularMolecular Sequence DataPhosphatidylinositolsProtein BindingProtein ConformationProtein Interaction Domains and MotifsScattering, Small AngleSequence AlignmentSorting NexinsPhosphatidylinositolsSNX20 protein, mouseSNX21 protein, mouseSorting Nexinsendosomemembrane traffickingphosphoinositidesmall-angle x-ray scattering (SAXS)sorting nexintetratricopeptide repeatX-ray crystallography

Identifiers

PMID25882846
PMCPMC4505518
OpenAlexW2052264626

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.