Evidence map›Paper›PMID 22675472›Full record

ArticlePloS one2012

Protein phosphatase-1α interacts with and dephosphorylates polycystin-1.

Stephen C Parnell, Sanjeev Puri, Darren P Wallace, James P Calvet

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. 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
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. 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

4 authors at 2 institutions in 2 countries.

Stephen C ParnellDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas, United States of America. sparnell@kumc.edu
Sanjeev Puri
Darren P Wallace
James P Calvet
University of Kansas Medical Center · USPanjab University · IN

Funding

ROLE OF OXIDANT STRESS IN PROGRESSION OF PKDP50DK057301 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI CALVET, JAMES P · 1999 to 2009
$11.3M
NIDDK NIH HHS P50 DK057301
6 · The paper itself

Abstract

Polycystin signaling is likely to be regulated by phosphorylation. While a number of potential protein kinases and their target phosphorylation sites on polycystin-1 have been identified, the corresponding phosphatases have not been extensively studied. We have now determined that polycystin-1 is a regulatory subunit for protein phosphatase-1α (PP1α). Sequence analysis has revealed the presence of a highly conserved PP1-interaction motif in the cytosolic, C-terminal tail of polycystin-1; and we have shown that transfected PP1α specifically co-immunoprecipitates with a polycystin-1 C-tail construct. To determine whether PP1α dephosphorylates polycystin-1, a PKA-phosphorylated GST-polycystin-1 fusion protein was shown to be dephosphorylated by PP1α but not by PP2B (calcineurin). Mutations within the PP1-binding motif of polycystin-1, including an autosomal dominant polycystic kidney disease (ADPKD)-associated mutation, significantly reduced PP1α-mediated dephosphorylation of polycystin-1. The results suggest that polycystin-1 forms a holoenzyme complex with PP1α via a conserved PP1-binding motif within the polycystin-1 C-tail, and that PKA-phosphorylated polycystin-1 serves as a substrate for the holoenzyme.

Indexed as

Amino Acid MotifsAmino AcidsAmino Acid SequenceAnimalsHEK293 CellsHoloenzymesHumansImmunoprecipitationMiceModels, BiologicalMolecular Sequence DataMutationPhosphorylationProtein BindingProtein Phosphatase 1Recombinant Fusion ProteinsAmino AcidsHoloenzymesProtein Phosphatase 1Recombinant Fusion ProteinsTRPP Cation Channels

Identifiers

PMID22675472
PMCPMC3366979
OpenAlexW2000377085

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.