Evidence map›Paper›PMID 24121510›Full record

ArticleThe Journal of biological chemistry2013

Role of AKAP79/150 protein in β1-adrenergic receptor trafficking and signaling in mammalian cells.

Xin Li, Mohammed M Nooh, Suleiman W Bahouth

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 46 citations in OpenAlex.

  1. β-Adrenergic Receptors: Not Always Outside-In.Physiology (Bethesda, Md.) · 2026
    Review
  2. Article
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  15. Review
  16. Novel Paradigms GoverningMolecular pharmacology · 2018
    Article
  17. Article
  18. Using cAMP Sensors to Study Cardiac Nanodomains.Journal of cardiovascular development and disease · 2018
    Review
  19. Review
  20. Function of Adenylyl Cyclase in Heart: the AKAP Connection.Journal of cardiovascular development and disease · 2018
    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

3 authors at 2 institutions in 1 country.

Xin LiDepartment of Pharmacology, University of Tennessee Health Sciences Center, Memphis, Tennessee 38163.
Mohammed M NoohDepartment of Pharmacology, University of Tennessee Health Sciences Center, Memphis, Tennessee 38163.
Suleiman W BahouthDepartment of Pharmacology, University of Tennessee Health Sciences Center, Memphis, Tennessee 38163. Electronic address: sbahouth@uthsc.edu.
University of Tennessee Health Science Center · USUniversity of Tennessee at Knoxville · US

Funding

PKA targeting: A novel mechanism for GPCR resensitizationR01HL085848 · NHLBI · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI BAHOUTH, SULEIMAN WAKIM · 2009 to 2012
$1.5M
NHLBI NIH HHS HL-085848NHLBI NIH HHS R01 HL085848
6 · The paper itself

Abstract

Protein kinase A-anchoring proteins (AKAPs) participate in the formation of macromolecular signaling complexes that include protein kinases, ion channels, effector enzymes, and G-protein-coupled receptors. We examined the role of AKAP79/150 (AKAP5) in trafficking and signaling of the β1-adrenergic receptor (β1-AR). shRNA-mediated down-regulation of AKAP5 in HEK-293 cells inhibited the recycling of the β1-AR. Recycling of the β1-AR in AKAP5 knockdown cells was rescued by shRNA-resistant AKAP5. However, truncated mutants of AKAP5 with deletions in the domains involved in membrane targeting or in binding to calcineurin or PKA failed to restore the recycling of the β1-AR, indicating that full-length AKAP5 was required. Furthermore, recycling of the β1-AR in rat neonatal cardiac myocytes was dependent on targeting the AKAP5-PKA complex to the C-terminal tail of the β1-AR. To analyze the role of AKAP5 more directly, recycling of the β1-AR was determined in ventricular myocytes from AKAP5(-/-) mice. In AKAP5(-/-) myocytes, the agonist-internalized β1-AR did not recycle, except when full-length AKAP5 was reintroduced. These data indicate that AKAP5 exerted specific and profound effects on β1-AR recycling in mammalian cells. Biochemical or real time FRET-based imaging of cyclic AMP revealed that deletion of AKAP5 sensitized the cardiac β1-AR signaling pathway to isoproterenol. Moreover, isoproterenol-mediated increase in contraction rate, surface area, or expression of β-myosin heavy chains was significantly greater in AKAP5(-/-) myocytes than in AKAP5(+/+) myocytes. These results indicate a significant role for the AKAP5 scaffold in signaling and trafficking of the β1-AR in cardiac myocytes and mammalian cells.

Indexed as

Adrenergic beta-1 Receptor AgonistsA Kinase Anchor ProteinsAmino Acid SequenceAnimalsCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansIsoproterenolMiceMice, KnockoutMyocytes, CardiacMyosin Heavy ChainsProtein TransportRatsReceptors, Adrenergic, beta-1Sequence DeletionAdrenergic beta-1 Receptor AgonistsAKAP5 protein, humanAkap5 protein, mouseAkap5 protein, ratA Kinase Anchor ProteinsCyclic AMP-Dependent Protein KinasesIsoproterenolMyosin Heavy ChainsReceptors, Adrenergic, beta-1Adrenergic ReceptorAKAPCyclic AMP (cAMP)Fluorescence Resonance Energy Transfer (FRET)G-protein-coupled Receptors (GPCR)Protein Kinase A (PKA)Receptor RecyclingTrafficking

Identifiers

PMID24121510
PMCPMC3837123
OpenAlexW1964463805

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.