Evidence map›Paper›PMID 17053785›Full record

ArticleThe EMBO journal2006

Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling.

Yiguo Wang, Dan Du, Longhou Fang, Guang Yang, Chenyi Zhang, Rong Zeng, Axel Ullrich, Friedrich Lottspeich, Zhengjun Chen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 79 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Tight junctions and their regulation by non-coding RNAs.International journal of biological sciences · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Adherens Junction and E-Cadherin complex regulation by epithelial polarity.Cellular and molecular life sciences : CMLS · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  15. Actin-interacting protein 1 controls assembly and permeability of intestinal epithelial apical junctions.American journal of physiology. Gastrointestinal and liver physiology · 2015
    Article
  16. Article
  17. Article
  18. Endocytosis and cancer.Cold Spring Harbor perspectives in biology · 2013
    Review
  19. ERK2-mediated phosphorylation of Par3 regulates neuronal polarization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    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

9 authors at 4 institutions in 2 countries.

Yiguo WangKey Laboratory of Proteomics and Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
Dan Du
Longhou Fang
Guang Yang
Chenyi Zhang
Rong Zeng
Axel Ullrich
Friedrich Lottspeich
Zhengjun Chen
Chinese Academy of Sciences · CNMax Planck Institute of Biochemistry · DEShanghai Institutes for Biological Sciences · CNCenter for Excellence in Molecular Cell Science · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved polarity complex, comprising the partitioning-defective (Par) proteins Par3 and Par6, and the atypical protein kinase C, functions in various cell-polarization events and asymmetric cell divisions. However, little is known about whether and how external stimuli-induced signals may regulate Par3 function in epithelial cell polarity. Here, we found that Par3 was tyrosine phosphorylated through phosphoproteomic profiling of pervanadate-induced phosphotyrosine proteins. We also demonstrated that the tyrosine phosphorylation event induced by multiple growth factors including epidermal growth factor (EGF) was dependent on activation of Src family kinase (SFK) members c-Src and c-Yes. The tyrosine residue 1127 (Y1127) of Par3 was identified as the major EGF-induced phosphorylation site. Moreover, we found that Y1127 phosphorylation reduced the association of Par3 with LIM kinase 2 (LIMK2), thus enabling LIMK2 to regulate cofilin phosphorylation dynamics. Substitution of Y1127 for phenylalanine impaired the EGF-induced Par3 and LIMK2 dissociation and delayed epithelial tight junction (TJ) assembly considerably. Collectively, these data suggest a novel, phosphotyrosine-dependent fine-tuning mechanism of Par3 in epithelial TJ assembly controlled by the EGF receptor-SFK signaling pathway.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SubstitutionAnimalsCarrier ProteinsCell Cycle ProteinsCell LineCell PolarityDogsEpithelial CellsErbB ReceptorsHumansMembrane ProteinsMutation, MissensePhosphorylationProtein KinasesProtein Processing, Post-TranslationalAdaptor Proteins, Signal TransducingCarrier ProteinsCell Cycle ProteinsErbB ReceptorsMembrane ProteinsPARD3 protein, humanPARD6A protein, humanProtein KinasesTyrosine

Identifiers

PMID17053785
PMCPMC1630420
OpenAlexW2102949950

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.