Evidence map›Paper›PMID 21126580›Full record

ArticleBiochimica et biophysica acta2011

Receptor protein tyrosine phosphatases are novel components of a polycystin complex.

Catherine A Boucher, Heather H Ward, Ruth L Case, Katie S Thurston, Xiaohong Li, Andrew Needham, Elsa Romero, Deborah Hyink, Seema Qamar, Tamara Roitbak and 5 more

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. 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
  6. Review
  7. Article
  8. Article
  9. The cleaved cytoplasmic tail of polycystin-1 regulates Src-dependent STAT3 activation.Journal of the American Society of Nephrology : JASN · 2014
    Article
  10. Review
  11. Article
  12. Article
  13. The extracellular matrix and ciliary signaling.Current opinion in cell biology · 2012
    Review
  14. Article
  15. Article
  16. Review
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

15 authors at 3 institutions in 1 country.

Catherine A BoucherDepartment of Medical Genetics, Cambridge Institute for Medical Research, Cambridge, CB2 2XY, UK.
Heather H Ward
Ruth L Case
Katie S Thurston
Xiaohong Li
Andrew Needham
Elsa Romero
Deborah Hyink
Seema Qamar
Tamara Roitbak
Samantha Powell
Christopher Ward
Patricia D Wilson
Angela Wandinger-Ness
Richard N Sandford
University of New Mexico · USIcahn School of Medicine at Mount Sinai · USMayo Clinic in Arizona · US

Funding

Viral Vector, Cell Line, Tissue & Mouse Model Production, Validation & ProcessingP01DK062345 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI WILSON, PATRICIA D. · 2003 to 2007
$6.7M
Pathologic Mechanisms of Polycystic Kidney DiseaseR01DK050141 · NIDDK · UNIVERSITY OF NEW MEXICO · PI WANDINGER-NESS, ANGELA · 1995 to 2010
$2.7M
Advanced Microscopy Shared Resource FacilityR24CA095823 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI FRIEDRICH, VICTOR LOUIS · 2002 to 2006
$1.3M
CONFOCAL MICROSCOPE FACILITYS10RR009145 · NCRR · MOUNT SINAI SCHOOL OF MEDICINE OF CUNY · PI MASUR, SANDRA K · 1994 to 1994
–
NCI NIH HHS 5R24 CA095823-04NCI NIH HHS R24 CA095823NCRR NIH HHS 1 S10 RR09145-01NIDDK NIH HHS DK P0162345NIDDK NIH HHS R01 DK050141NIDDK NIH HHS R01 DK50141Wellcome Trust
6 · The paper itself

Abstract

Autosomal dominant polycystic kidney disease (ADPKD) is caused by mutation of PKD1 and PKD2 that encode polycystin-1 and polycystin-2. Polycystin-1 is tyrosine phosphorylated and modulates multiple signaling pathways including AP-1, and the identity of the phosphatases regulating polycystin-1 are previously uncharacterized. Here we identify members of the LAR protein tyrosine phosphatase (RPTP) superfamily as members of the polycystin-1complex mediated through extra- and intracellular interactions. The first extracellular PKD1 domain of polycystin-1 interacts with the first Ig domain of RPTPσ, while the polycystin-1 C-terminus of polycystin-1 interacts with the regulatory D2 phosphatase domain of RPTPγ. Additional homo- and heterotypic interactions between RPTPs recruit RPTPδ. The multimeric polycystin protein complex is found localised in cilia. RPTPσ and RPTPδ are also part of a polycystin-1/E-cadherin complex known to be important for early events in adherens junction stabilisation. The interaction between polycystin-1 and RPTPγ is disrupted in ADPKD cells, while RPTPσ and RPTPδ remain closely associated with E-cadherin, largely in an intracellular location. The polycystin-1 C-terminus is an in vitro substrate of RPTPγ, which dephosphorylates the c-Src phosphorylated Y4237 residue and activates AP1-mediated transcription. The data identify RPTPs as novel interacting partners of the polycystins both in cilia and at adhesion complexes and demonstrate RPTPγ phosphatase activity is central to the molecular mechanisms governing polycystin-dependent signaling. This article is part of a Special Issue entitled: Polycystic Kidney Disease.

Indexed as

Amino Acid SequenceAnimalsCadherinsCell LineCell MembraneHumansIn Vitro TechniquesKidneyMiceModels, MolecularMultiprotein ComplexesMutagenesis, Site-DirectedPeptide LibraryPolycystic Kidney, Autosomal DominantProtein Interaction Domains and MotifsReceptor-Like Protein Tyrosine PhosphatasesCadherinsMultiprotein ComplexesPeptide LibraryReceptor-Like Protein Tyrosine PhosphatasesReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 5Recombinant ProteinsTranscription Factor AP-1TRPP Cation Channels

Identifiers

PMID21126580
PMCPMC3156852
OpenAlexW2105638087

What OpenQuestion holds

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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.