Evidence map›Paper›PMID 21680711›Full record

ArticleMolecular biology of the cell2011

Confinement of β(1)- and β(2)-adrenergic receptors in the plasma membrane of cardiomyocyte-like H9c2 cells is mediated by selective interactions with PDZ domain and A-kinase anchoring proteins but not caveolae.

Cathleen D Valentine, Peter M Haggie

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Tetramisole is a new IPharmacology research & perspectives · 2022
    Review
  5. Review
  6. Components of the GTraffic (Copenhagen, Denmark) · 2020
    Article
  7. Imaging cAMP nanodomains in the heart.Biochemical Society transactions · 2019
    Review
  8. Regulation of monoamine transporters and receptors by lipid microdomains: implications for depression.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018
    Review
  9. Review
  10. Novel Paradigms GoverningMolecular pharmacology · 2018
    Article
  11. Review
  12. Article
  13. Beta1-adrenergic receptor-mediated dilation of rat cerebral artery requires Shaker-type KV1 channels on PSD95 scaffold.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Reprogramming of G protein-coupled receptor recycling and signaling by a kinase switch.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Cathleen D ValentineDivision of Nephrology, Department of Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Peter M Haggie

Funding

LIVE-CELL IMAGING OF CFTR OLIGOMERIZATION, TRAFFICKING AND INTERACTIONSR01DK081355 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HAGGIE, PETER MICHAEL · 2008 to 2012
$1.5M
NIDDK NIH HHS DK 081355NIDDK NIH HHS R01 DK081355
6 · The paper itself

Abstract

The sympathetic nervous system regulates cardiac output by activating adrenergic receptors (ARs) in cardiac myocytes. The predominant cardiac ARs, β(1)- and β(2)AR, are structurally similar but mediate distinct signaling responses. Scaffold protein-mediated compartmentalization of ARs into discrete, multiprotein complexes has been proposed to dictate differential signaling responses. To test the hypothesis that βARs integrate into complexes in live cells, we measured receptor diffusion and interactions by single-particle tracking. Unstimulated β(1)- and β(2)AR were highly confined in the membrane of H9c2 cardiomyocyte-like cells, indicating that receptors are tethered and presumably integrated into protein complexes. Selective disruption of interactions with postsynaptic density protein 95/disks large/zonula occludens-1 (PDZ)-domain proteins and A-kinase anchoring proteins (AKAPs) increased receptor diffusion, indicating that these scaffold proteins participate in receptor confinement. In contrast, modulation of interactions between the putative scaffold caveolae and β(2)AR did not alter receptor dynamics, suggesting that these membrane domains are not involved in β(2)AR confinement. For both β(1)- and β(2)AR, the receptor carboxy-terminus was uniquely responsible for scaffold interactions. Our data formally demonstrate that distinct and stable protein complexes containing β(1)- or β(2)AR are formed in the plasma membrane of cardiomyocyte-like cells and that selective PDZ and AKAP interactions are responsible for the integration of receptors into complexes.

Indexed as

Actin CytoskeletonActinsA Kinase Anchor ProteinsAnimalsCaveolaeCell LineChlorocebus aethiopsFluorescence Recovery After PhotobleachingHumansMicroscopy, FluorescenceMyocytes, CardiacPDZ DomainsPeptide FragmentsProtein BindingRatsReceptors, Adrenergic, beta-1ActinsA Kinase Anchor ProteinsPeptide FragmentsReceptors, Adrenergic, beta-1Receptors, Adrenergic, beta-2

Identifiers

PMID21680711
PMCPMC3154891

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.