Evidence map›Paper›PMID 23826934›Full record

ArticleThe Biochemical journal2013

Sorting nexin 27 (SNX27) associates with zonula occludens-2 (ZO-2) and modulates the epithelial tight junction.

Seth P Zimmerman, Christina L Hueschen, Daniela Malide, Sharon L Milgram, Martin P Playford

Abstract read
In one paragraph

Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Papillomaviruses and Endocytic Trafficking.International journal of molecular sciences · 2018
    Review
  10. Article
  11. Review
  12. Article
  13. [Progressive familial intrahepatic cholestasis related to mutation of the TJP2 gene: recent advances].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2016
    Article
  14. Article
  15. Sorting Nexin 27 regulates basal and activity-dependent trafficking of AMPARs.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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 2 institutions in 1 country.

Seth P Zimmerman*Cell Biology and Physiology Center, National Institutes of Health, Bethesda, MD 20982, U.S.A.
Christina L Hueschen
Daniela Malide
Sharon L Milgram
Martin P Playford
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

Light Microscopy CoreZICHL006019 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI COMBS, CHRISTIAN · 2009 to 2025
$29.3M
Intramural NIH HHS Z99 HL999999
6 · The paper itself

Abstract

Proteins of the SNX (sorting nexin) superfamily are characterized by the presence of a PX (Phox homology) domain and associate with PtdIns3P (phosphatidylinositol-3-monophosphate)-rich regions of the endosomal system. SNX27 is the only sorting nexin that contains a PDZ domain. In the present study, we used a proteomic approach to identify a novel interaction between SNX27 and ZO-2 [zonula occludens-2; also known as TJP2 (tight junction protein 2)], a component of the epithelial tight junction. The SNX27-ZO-2 interaction requires the PDZ domain of SNX27 and the C-terminal PDZ-binding motif of ZO-2. When tight junctions were perturbed by chelation of extracellular Ca2+, ZO-2 transiently localized to SNX27-positive early endosomes. Depletion of SNX27 in mpkCCD (mouse primary kidney cortical collecting duct) cell monolayers resulted in a decrease in the rate of ZO-2, but not ZO-1, mobility at cell-cell contact regions after photobleaching and an increase in junctional permeability to large solutes. The findings of the present study identify an important new SNX27-binding partner and suggest a role for endocytic pathways in the intracellular trafficking of ZO-2 and possibly other tight junction proteins. Our results also indicate a role for SNX27-ZO-2 interactions in tight junction maintenance and function.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBiological TransportEndocytosisEpithelial CellsGene Expression RegulationKidney Tubules, CollectingMiceMolecular Sequence DataPrimary Cell CultureProtein BindingProtein Structure, TertiarySignal TransductionSorting NexinsTight JunctionsSnx27 protein, mouseSorting NexinsTjp1 protein, mouseTjp2 protein, mouseZonula Occludens-1 ProteinZonula Occludens-2 Protein

Identifiers

PMID23826934
PMCPMC4285712
OpenAlexW2333438127

What OpenQuestion holds

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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.