Evidence map›Paper›PMID 18048357›Full record

ArticleThe Journal of biological chemistry2008

The alpha1a-adrenergic receptor occupies membrane rafts with its G protein effectors but internalizes via clathrin-coated pits.

Daniel P Morris, Beilei Lei, Yue-Xuan Wu, Gregory A Michelotti, Debra A Schwinn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Drug target insights · 2020
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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 at 3 institutions in 1 country.

Daniel P MorrisDepartment of Anesthesiology, Duke University Medical Center, 595 LaSalle Street, Durham, NC 27710, USA. morri082@mc.duke.edu
Beilei Lei
Yue-Xuan Wu
Gregory A Michelotti
Debra A Schwinn
Duke University Hospital · USDuke Medical Center · USUniversity of Washington · US

Funding

Subcellular Distribution &Regulation of ala-AdrenoceptoR37HL049103 · NHLBI · UNIVERSITY OF WASHINGTON · PI SCHWINN, DEBRA ANNE · 2005 to 2014
$3.9M
MOLECULAR DISTRIBUTION OF HUMAN ADRENERGIC RECEPTORSR01HL049103 · NHLBI · DUKE UNIVERSITY · PI SCHWINN, DEBRA A. · 1993 to 2003
$1.4M
NHLBI NIH HHS HL 49103NHLBI NIH HHS R01 HL049103NHLBI NIH HHS R37 HL049103
6 · The paper itself

Abstract

The alpha(1a)-adrenergic receptor (alpha(1a)AR) occupies intracellular and plasma membranes in both native and heterologous expression systems. Based on multiple independent lines of evidence, we demonstrate the alpha(1a)AR at the cell surface occupies membrane rafts but exits from rafts following stimulation. In non-detergent raft preparations, basal alpha(1a)AR is present in low density membrane rafts and colocalizes with its G protein effectors on density gradients. Raft disruption by cholesterol depletion with methyl-beta-cyclodextrin eliminates these light rafts. To confirm the presence of the alpha(1a)AR in plasma membrane rafts, fluorescence resonance energy transfer measurements were used to demonstrate colocalization of surface receptor and the raft marker, cholera toxin B. This colocalization was largely lost following alpha(1a)AR stimulation with phenylephrine. Similarly, receptor stimulation causes exit of the alpha(1a)AR from light rafts within 3-10 min in contrast to the G proteins, which largely remain in light rafts. Importantly, this delayed exit of the alpha(1a)AR suggests acute receptor signaling and desensitization occur entirely within rafts. Interestingly, both confocal analysis and measurement of surface alpha(1a)AR levels indicate modest receptor internalization during the 10 min following stimulation, suggesting most of the receptor has entered non-raft plasma membrane. Nevertheless, activation does increase the rate of receptor internalization as does disruption of rafts with methyl-beta-cyclodextrin, suggesting raft exit enables internalization. Confocal analysis of surface-labeled hemagglutinin-alpha(1a)AR reveals that basal and stimulated receptor occupies clathrin pits in fixed cells consistent with previous indirect evidence. The evidence presented here strongly suggests the alpha(1a)AR is a lipid raft protein under basal conditions and implies agonist-mediated signaling occurs from rafts.

Indexed as

Animalsbeta-CyclodextrinsCell LineCholera ToxinCholesterolCoated Pits, Cell-MembraneFluorescence Resonance Energy TransferGTP-Binding ProteinsHumansMembrane MicrodomainsPhenylephrineRatsReceptors, Adrenergic, alpha-1Recombinant Fusion ProteinsSignal Transductionbeta-CyclodextrinsCholera ToxinCholesterolGTP-Binding Proteinsmethyl-beta-cyclodextrinPhenylephrineReceptors, Adrenergic, alpha-1Recombinant Fusion Proteins

Identifiers

PMID18048357
PMCPMC2566898
OpenAlexW1992528187

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.