Evidence map›Paper›PMID 21464135›Full record

ArticleThe Journal of biological chemistry2011

Differential regulation of two palmitoylation sites in the cytoplasmic tail of the beta1-adrenergic receptor.

David M Zuckerman, Stuart W Hicks, Guillaume Charron, Howard C Hang, Carolyn E Machamer

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. ProteinOpen biology · 2021
    Review
  6. Review
  7. Article
  8. β-blockers Reverse Agonist-Induced βInternational journal of molecular sciences · 2020
    Article
  9. Article
  10. DifferentialThe Journal of biological chemistry · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Palmitoyl acyltransferase Aph2 in cardiac function and the development of cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. The physiology of protein S-acylation.Physiological reviews · 2015
    Review
  18. Article
  19. Article
  20. 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

5 authors.

David M ZuckermanDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Stuart W Hicks
Guillaume Charron
Howard C Hang
Carolyn E Machamer

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Studies on Protein LipidationR01GM087544 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HANG, HOWARD C · 2010 to 2023
$4.4M
TARGETING AND RETENTION OF GOLGI MEMBRANE PROTEINSR01GM042522 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MACHAMER, CAROLYN E · 1989 to 2011
$3.1M
S. typhimurium leucine-rich repeat effector proteinsF32AI069704 · NIAID · YALE UNIVERSITY · PI HICKS, STUART W · 2007 to 2009
$154k
NIAID NIH HHS AI069704NIAID NIH HHS F32 AI069704NIGMS NIH HHS 1R01GM087544NIGMS NIH HHS GM42522NIGMS NIH HHS R01 GM042522NIGMS NIH HHS R01 GM087544NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

S-Palmitoylation of G protein-coupled receptors (GPCRs) is a prevalent modification, contributing to the regulation of receptor function. Despite its importance, the palmitoylation status of the β(1)-adrenergic receptor, a GPCR critical for heart function, has never been determined. We report here that the β(1)-adrenergic receptor is palmitoylated on three cysteine residues at two sites in the C-terminal tail. One site (proximal) is adjacent to the seventh transmembrane domain and is a consensus site for GPCRs, and the other (distal) is downstream. These sites are modified in different cellular compartments, and the distal palmitoylation site contributes to efficient internalization of the receptor following agonist stimulation. Using a bioorthogonal palmitate reporter to quantify palmitoylation accurately, we found that the rates of palmitate turnover at each site are dramatically different. Although palmitoylation at the proximal site is remarkably stable, palmitoylation at the distal site is rapidly turned over. This is the first report documenting differential dynamics of palmitoylation sites in a GPCR. Our results have important implications for function and regulation of the clinically important β(1)-adrenergic receptor.

Indexed as

CysteineHEK293 CellsHumansLipoylationProtein Processing, Post-TranslationalProtein Structure, TertiaryReceptors, Adrenergic, beta-1CysteineReceptors, Adrenergic, beta-1

Identifiers

PMID21464135
PMCPMC3099716

What OpenQuestion holds

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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.