Evidence map›Paper›PMID 17332505›Full record

ArticleMolecular biology of the cell2007

A bipartite signal regulates the faithful delivery of apical domain marker podocalyxin/Gp135.

Chun-Ying Yu, Jen-Yau Chen, Yu-Yu Lin, Kuo-Fang Shen, Wei-Ling Lin, Chung-Liang Chien, Martin B A ter Beest, Tzuu-Shuh Jou

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Loss of mucin-typeThe Journal of biological chemistry · 2017
    Article
  8. Article
  9. Typhoid toxin provides a window into typhoid fever and the biology of Salmonella Typhi.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Review
  10. Article
  11. Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014
    Review
  12. Article
  13. Article
  14. Membrane trafficking in podocyte health and disease.Pediatric nephrology (Berlin, Germany) · 2013
    Review
  15. Article
  16. Snail destabilizes cell surface Crumbs3a.Traffic (Copenhagen, Denmark) · 2012
    Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 3 institutions in 2 countries.

Chun-Ying YuDepartment of Internal Medicine, National Taiwan University Hospital, National Taiwan University College of Medicine, Taipei, 100 Taiwan.
Jen-Yau Chen
Yu-Yu Lin
Kuo-Fang Shen
Wei-Ling Lin
Chung-Liang Chien
Martin B A ter Beest
Tzuu-Shuh Jou
National Taiwan University Hospital · TWNational Taiwan University · TWUniversity of Cincinnati Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podocalyxin/Gp135 was recently demonstrated to participate in the formation of a preapical complex to set up initial polarity in MDCK cells, a function presumably depending on the apical targeting of Gp135. We show that correct apical sorting of Gp135 depends on a bipartite signal composed of an extracellular O-glycosylation-rich region and the intracellular PDZ domain-binding motif. The function of this PDZ-binding motif could be substituted with a fusion construct of Gp135 with Ezrin-binding phosphoprotein 50 (EBP50). In accordance with this observation, EBP50 binds to newly synthesized Gp135 at the Golgi apparatus and facilitates oligomerization and sorting of Gp135 into a clustering complex. A defective connection between Gp135 and EBP50 or EBP50 knockdown results in a delayed exit from the detergent-resistant microdomain, failure of oligomerization, and basolateral missorting of Gp135. Furthermore, the basolaterally missorted EBP50-binding defective mutant of Gp135 was rapidly retrieved via a PKC-dependent mechanism. According to these findings, we propose a model by which a highly negative charged transmembrane protein could be packed into an apical sorting platform with the aid of its cytoplasmic partner EBP50.

Indexed as

Amino Acid MotifsAnimalsBase SequenceBinding SitesCarrier ProteinsCell PolarityCells, CulturedCytoskeletal ProteinsDogsEndocytosisEzrinGlycosylationMembrane MicrodomainsModels, BiologicalMutationProtein Kinase CCarrier ProteinsCytoskeletal ProteinsEzrinpodocalyxinProtein Kinase CProtein Sorting SignalsRNA, Small InterferingSialoglycoproteins

Identifiers

PMID17332505
PMCPMC1855014
OpenAlexW2145341973

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.