Evidence map›Paper›PMID 20819076›Full record

ArticleThe Biochemical journal2010

Interaction with receptor for activated C-kinase 1 (RACK1) sensitizes the phosphodiesterase PDE4D5 towards hydrolysis of cAMP and activation by protein kinase C.

Rebecca J Bird, George S Baillie, Stephen J Yarwood

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2010. 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
1.1field-weighted citation impact, top 23% 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, 35 citations in OpenAlex.

  1. Review
  2. PDE4D: A Multipurpose Pharmacological Target.International journal of molecular sciences · 2024
    Review
  3. Article
  4. Article
  5. Transcriptomic analysis ofBiology open · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Maize ZmRACK1 is involved in the plant response to fungal phytopathogens.International journal of molecular sciences · 2014
    Article
  16. Article
  17. RACK1/Asc1p, a ribosomal node in cellular signaling.Molecular & cellular proteomics : MCP · 2013
    Article
  18. Review
  19. RACK1, A multifaceted scaffolding protein: Structure and function.Cell communication and signaling : CCS · 2011
    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

3 authors at 1 institution in 1 country.

Rebecca J BirdInstitute of Molecular Cell and Systems Biology, University of Glasgow, Scotland, UK.
George S Baillie
Stephen J Yarwood
University of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D015324/1British Heart Foundation PG/10/026/28303British Heart Foundation PG/10/26/28303
6 · The paper itself

Abstract

We have previously identified the PKC (protein kinase C)-anchoring protein RACK1 (receptor for activated C-kinase 1), as a specific binding partner for the cAMP-specific phosphodiesterase PDE4D5, suggesting a potential site for cross-talk between the PKC and cAMP signalling pathways. In the present study we found that elevation of intracellular cAMP, with the β₂-adrenoceptor agonist isoproterenol (isoprenaline), led to activation of PDE4 enzymes in the particulate and soluble fractions of HEK (human embryonic kidney)-293 cells. In contrast activation of PDE4D5, with isoproterenol and the PKC activator PMA, was restricted to the particulate fraction, where it interacts with RACK1; however, RACK1 is dispensable for anchoring PDE4D5 to the particulate fraction. Kinetic studies demonstrated that RACK1 alters the conformation of particulate-associated PDE4D5 so that it more readily interacts with its substrate cAMP and with rolipram, a PDE4 inhibitor that specifically targets the active site of the enzyme. Interaction with RACK1 was also essential for PKC-dependent and ERK (extracellular-signal-regulated kinase)-independent phosphorylation (on Ser¹²⁶), and activation of PDE4D5 in response to PMA and isoproterenol, both of which trigger the recruitment of PKCα to RACK1. Together these results reveal novel signalling cross-talk, whereby RACK1 mediates PKC-dependent activation of PDE4D5 in the particulate fraction of HEK-293 cells in response to elevations in intracellular cAMP.

Indexed as

Binding SitesBlotting, WesternCyclic AMPCyclic Nucleotide Phosphodiesterases, Type 3Cyclic Nucleotide Phosphodiesterases, Type 4Enzyme ActivationGTP-Binding ProteinsHEK293 CellsHumansHydrolysisIntracellular SpaceIsoproterenolKineticsMutationNeoplasm ProteinsPhosphodiesterase 4 InhibitorsCyclic AMPCyclic Nucleotide Phosphodiesterases, Type 3Cyclic Nucleotide Phosphodiesterases, Type 4GTP-Binding ProteinsIsoproterenolNeoplasm ProteinsPDE4D protein, humanPhosphodiesterase 4 InhibitorsProtein Kinase CProtein Kinase C-alphaRACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C KinaseRolipramTetradecanoylphorbol Acetate

Identifiers

PMID20819076
PMCPMC2973232
OpenAlexW2154895648

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.