Evidence map›Paper›PMID 21357695›Full record

ArticleThe Journal of biological chemistry2011

Alpha2B-adrenergic receptor interaction with tubulin controls its transport from the endoplasmic reticulum to the cell surface.

Matthew T Duvernay, Hong Wang, Chunmin Dong, Jesse J Guidry, Dan L Sackett, Guangyu Wu

Open access · hybridAbstract 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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
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  11. Article
  12. Review
  13. Article
  14. Luminal ANG II is internalized as a complex with ATAmerican journal of physiology. Renal physiology · 2017
    Article
  15. Article
  16. Article
  17. Regulation of α2B-Adrenerigc Receptor Export Trafficking by Specific Motifs.Progress in molecular biology and translational science · 2015
    Review
  18. Article
  19. Article
  20. Cell Cycle Regulation of the Centrosome and Cilium.Drug discovery today. Disease mechanisms · 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

6 authors at 3 institutions in 2 countries.

Matthew T DuvernayFrom the Department of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112.
Hong Wang
Chunmin Dong
Jesse J Guidry
Dan L Sackett
Guangyu Wu
Louisiana State University Health Sciences Center New Orleans · USEunice Kennedy Shriver National Institute of Child Health and Human Development · USTongji University · CN

Funding

VASCULAR SMOOTH MUSCLE PLASTICITY IN NITRIC OXIDEP20RR018766 · NCRR · LSU HEALTH SCIENCES CENTER · PI KAPUSTA, DANIEL R · 2003 to 2011
$18.5M
Microtubule regulation by small molecules.ZIAHD008765 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SACKETT, DAN L · 2009 to 2025
$8.9M
ER-to-Golgi traffic and signal regulation of GPCRsR01GM076167 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WU, GUANGYU · 2006 to 2013
$2.2M
Intramural NIH HHSNCRR NIH HHS P20 RR018766NCRR NIH HHS P20RR018766NIGMS NIH HHS R01 GM076167NIGMS NIH HHS R01GM076167
6 · The paper itself

Abstract

It is well recognized that the C terminus (CT) plays a crucial role in modulating G protein-coupled receptor (GPCR) transport from the endoplasmic reticulum (ER) to the cell surface. However the molecular mechanisms that govern CT-dependent ER export remain elusive. To address this issue, we used α(2B)-adrenergic receptor (α(2B)-AR) as a model GPCR to search for proteins interacting with the CT. By using peptide-conjugated affinity matrix combined with proteomics and glutathione S-transferase fusion protein pull-down assays, we identified tubulin directly interacting with the α(2B)-AR CT. The interaction domains were mapped to the acidic CT of tubulin and the basic Arg residues in the α(2B)-AR CT, particularly Arg-437, Arg-441, and Arg-446. More importantly, mutation of these Arg residues to disrupt tubulin interaction markedly inhibited α(2B)-AR transport to the cell surface and strongly arrested the receptor in the ER. These data provide the first evidence indicating that the α(2B)-AR C-terminal Arg cluster mediates its association with tubulin to coordinate its ER-to-cell surface traffic and suggest a novel mechanism of GPCR export through physical contact with microtubules.

Indexed as

Amino Acid SequenceAnimalsCell MembraneEndoplasmic ReticulumGlutathione TransferaseHumansMicrotubulesMolecular Sequence DataProtein BindingProtein Structure, TertiaryProtein TransportRatsReceptors, Adrenergic, alpha-2Receptors, G-Protein-CoupledSequence Homology, Amino AcidTubulinGlutathione TransferaseReceptors, Adrenergic, alpha-2Receptors, G-Protein-CoupledTubulin

Identifiers

PMID21357695
PMCPMC3077609
OpenAlexW2019247237

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.