Evidence map›Paper›PMID 26311459›Full record

ArticleJournal of the American Society of Nephrology : JASN2016

The Polycystin-1, Lipoxygenase, and α-Toxin Domain Regulates Polycystin-1 Trafficking.

Yaoxian Xu, Andrew J Streets, Andrea M Hounslow, Uyen Tran, Frederic Jean-Alphonse, Andrew J Needham, Jean-Pierre Vilardaga, Oliver Wessely, Michael P Williamson, Albert C M Ong

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Society of Nephrology : JASN, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Polycystin Channel Complexes.Annual review of physiology · 2023
    Review
  6. The CommonHuman mutation · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022
    Review
  11. Biallelic inheritance of hypomorphic PKD1 variants is highly prevalent in very early onset polycystic kidney disease.Genetics in medicine : official journal of the American College of Medical Genetics · 2021
    Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Protein phosphatase 1α interacts with a novel ciliary targeting sequence of polycystin-1 and regulates polycystin-1 trafficking.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  17. Article
  18. Polycystic kidney disease.Nature reviews. Disease primers · 2018
    Review
  19. Characterization of Epidermal Lipoxygenase Expression in Normal Human Skin and Tissue-Engineered Skin Substitutes.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2018
    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

10 authors at 4 institutions in 2 countries.

Yaoxian XuKidney Genetics Group, Academic Nephrology Unit, University of Sheffield Medical School, Sheffield, United Kingdom; Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom;
Andrew J StreetsKidney Genetics Group, Academic Nephrology Unit, University of Sheffield Medical School, Sheffield, United Kingdom;
Andrea M HounslowDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom;
Uyen TranDepartment of Cellular and Molecular Medicine, Cleveland Clinic Foundation, Cleveland, Ohio; and.
Frederic Jean-AlphonseLaboratory of GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania.
Andrew J NeedhamKidney Genetics Group, Academic Nephrology Unit, University of Sheffield Medical School, Sheffield, United Kingdom;
Jean-Pierre VilardagaLaboratory of GPCR Biology, Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania.
Oliver WesselyDepartment of Cellular and Molecular Medicine, Cleveland Clinic Foundation, Cleveland, Ohio; and.
Michael P WilliamsonDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom;
Albert C M OngKidney Genetics Group, Academic Nephrology Unit, University of Sheffield Medical School, Sheffield, United Kingdom; a.ong@sheffield.ac.uk.
University of Sheffield · GBCleveland Clinic · USSheffield Kidney Institute · GBUniversity of Pittsburgh · US

Funding

Structural and Functional Mechanisms of PTH-Receptor SignalingR01DK102495 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO, GARDELLA, THOMAS J · 2014 to 2017
$2.0M
The Role of Bicaudal-C in Polycystic Kidney DiseaseR01DK080745 · NIDDK · LSU HEALTH SCIENCES CENTER · PI WESSELY, OLIVER · 2009 to 2013
$1.7M
Sustained cAMP Signals Triggered by Internalized PTH Receptor: New Consequences fR01DK087688 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VILARDAGA, JEAN-PIERRE · 2010 to 2014
$1.6M
Medical Research CouncilNIDDK NIH HHS R01 DK080745NIDDK NIH HHS R01-DK080745-05NIDDK NIH HHS R01 DK087688NIDDK NIH HHS R01-DK087688NIDDK NIH HHS R01 DK102495NIDDK NIH HHS R01-DK102495
6 · The paper itself

Abstract

Mutations in polycystin-1 (PC1) give rise to autosomal dominant polycystic kidney disease, an important and common cause of kidney failure. Despite its medical importance, the function of PC1 remains poorly understood. Here, we investigated the role of the intracellular polycystin-1, lipoxygenase, and α-toxin (PLAT) signature domain of PC1 using nuclear magnetic resonance, biochemical, cellular, and in vivo functional approaches. We found that the PLAT domain targets PC1 to the plasma membrane in polarized epithelial cells by a mechanism involving the selective binding of the PLAT domain to phosphatidylserine and L-α-phosphatidylinositol-4-phosphate (PI4P) enriched in the plasma membrane. This process is regulated by protein kinase A phosphorylation of the PLAT domain, which reduces PI4P binding and recruits β-arrestins and the clathrin adaptor AP2 to trigger PC1 internalization. Our results reveal a physiological role for the PC1-PLAT domain in renal epithelial cells and suggest that phosphorylation-dependent internalization of PC1 is closely linked to its function in renal development and homeostasis.

Indexed as

HumansLipoxygenaseMutationProtein Structure, TertiaryTRPP Cation ChannelsLipoxygenaseTRPP Cation Channelsautosomal dominant polycystic kidney diseasegenetics and developmentpolycystic kidney disease

Identifiers

PMID26311459
PMCPMC4814171
OpenAlexW2184067519

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.