Evidence map›Paper›PMID 27911714›Full record

ReviewBiochemical Society transactions2016

Regulation of the phosphatase PP2B by protein-protein interactions.

Patrick J Nygren, John D Scott

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Hydrogen Sulfide (HInternational journal of molecular sciences · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Calcineurin.Cell communication and signaling : CCS · 2020
    Review
  14. Article
  15. Identifying New Substrates and Functions for an Old Enzyme: Calcineurin.Cold Spring Harbor perspectives in biology · 2020
    Review
  16. Article
  17. Functions and therapeutic potential of protein phosphatase 1: Insights from mouse genetics.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Patrick J NygrenDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
John D ScottDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Howard Hughes Medical Institute · US

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Local Signaling in Diabetic ComorbiditiesR01DK105542 · NIDDK · UNIVERSITY OF WASHINGTON · PI SCOTT, JOHN D · 2015 to 2018
$1.4M
NIDDK NIH HHS P01 DK054441NIDDK NIH HHS R01 DK105542
6 · The paper itself

Abstract

Protein dephosphorylation is important for regulating cellular signaling in a variety of contexts. Protein phosphatase-2B (PP2B), or calcineurin, is a widely expressed serine/threonine phosphatase that acts on a large cross section of potential protein substrates when activated by increased levels of intracellular calcium in concert with calmodulin. PxIxIT and LxVP targeting motifs are important for maintaining specificity in response to elevated calcium. In the present study, we describe the mechanism of PP2B activation, discuss its targeting by conserved binding motifs and review recent advances in the understanding of an A-kinase anchoring protein 79/PP2B/protein kinase A complex's role in synaptic long-term depression. Finally, we discuss potential for targeting PP2B anchoring motifs for therapeutic benefit.

Indexed as

Long-Term Synaptic DepressionA Kinase Anchor ProteinsAnimalsCalcineurinCalciumCalmodulinCyclic AMP-Dependent Protein KinasesHumansModels, BiologicalProtein BindingAKAP5 protein, humanA Kinase Anchor ProteinsCalcineurinCalciumCalmodulinCyclic AMP-Dependent Protein KinasesAKAP79anchoring proteincalcineurinphosphatasePP2Bsynaptic plasticity

Identifiers

PMID27911714
PMCPMC5142753
OpenAlexW2533237926

What OpenQuestion holds

Textmetadata
LicenceTDM
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.