Evidence map›Paper›PMID 21423175›Full record

ArticleNature cell biology2011

Control of PKA stability and signalling by the RING ligase praja2.

Luca Lignitto, Annalisa Carlucci, Maria Sepe, Eduard Stefan, Ornella Cuomo, Robert Nisticò, Antonella Scorziello, Claudia Savoia, Corrado Garbi, Lucio Annunziato and 1 more

Abstract read
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In one paragraph

Article in Nature cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

58 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
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  4. Review
  5. Conformational Dynamics and Allostery in the cAMP-Protein Kinase A Signalosome.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Article
  8. PJA2 Suppresses Colorectal Cancer Progression by Controlling HDAC2 Degradation and Stability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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  18. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Luca LignittoDipartimento di Biologia e Patologia Cellulare e Molecolare L. Califano, Universitá Federico II, 80131 Naples, Italy.
Annalisa Carlucci
Maria Sepe
Eduard Stefan
Ornella Cuomo
Robert Nisticò
Antonella Scorziello
Claudia Savoia
Corrado Garbi
Lucio Annunziato
Antonio Feliciello
University of Naples Federico II · ITFondazione Santa Lucia · ITUniversität Innsbruck · AT

Funding

Austrian Science Fund FWF P 22608
6 · The paper itself

Abstract

Activation of G-protein-coupled receptors (GPCRs) mobilizes compartmentalized pulses of cyclic AMP. The main cellular effector of cAMP is protein kinase A (PKA), which is assembled as an inactive holoenzyme consisting of two regulatory (R) and two catalytic (PKAc) subunits. cAMP binding to R subunits dissociates the holoenzyme and releases the catalytic moiety, which phosphorylates a wide array of cellular proteins. Reassociation of PKAc and R components terminates the signal. Here we report that the RING ligase praja2 controls the stability of mammalian R subunits. Praja2 forms a stable complex with, and is phosphorylated by, PKA. Rising cAMP levels promote praja2-mediated ubiquitylation and subsequent proteolysis of compartmentalized R subunits, leading to sustained substrate phosphorylation by the activated kinase. Praja2 is required for efficient nuclear cAMP signalling and for PKA-mediated long-term memory. Thus, praja2 regulates the total concentration of R subunits, tuning the strength and duration of PKA signal output in response to cAMP.

Indexed as

Enzyme StabilityA Kinase Anchor ProteinsAnimalsCell Line, TumorCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinDNA-Binding ProteinsEnzyme ActivationHEK293 CellsHumansLong-Term PotentiationMiceNeuroblastomaNeuronsProtein SubunitsA Kinase Anchor ProteinsCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinDNA-Binding ProteinsPJA2 protein, mousePja2 protein, ratProtein SubunitsProto-Oncogene Proteins c-fosRecombinant Fusion ProteinsUbiquitin-Protein Ligases

Identifiers

PMID21423175
OpenAlexW2102267300

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.