Evidence map›Paper›PMID 19357319›Full record

ArticleThe Journal of pharmacology and experimental therapeutics2009

Rab1 GTPase and dimerization in the cell surface expression of angiotensin II type 2 receptor.

Xiaoping Zhang, Guansong Wang, Denis J Dupré, Yumei Feng, Mélanie Robitaille, Eric Lazartigues, Ying-Hong Feng, Terence E Hébert, Guangyu Wu

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of pharmacology and experimental therapeutics, 2009. 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
2.2field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Investigation of Receptor Heteromers Using NanoBRET Ligand Binding.International journal of molecular sciences · 2021
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Regulation of α2B-Adrenerigc Receptor Export Trafficking by Specific Motifs.Progress in molecular biology and translational science · 2015
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Small GTPase regulation of GPCR anterograde trafficking.Trends in pharmacological sciences · 2012
    Review
  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

9 authors at 3 institutions in 2 countries.

Xiaoping ZhangDepartment of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, 1901 Perdido St., New Orleans, LA 70112, USA.
Guansong Wang
Denis J Dupré
Yumei Feng
Mélanie Robitaille
Eric Lazartigues
Ying-Hong Feng
Terence E Hébert
Guangyu Wu
Louisiana State University Health Sciences Center New Orleans · USMcGill University · CAUniformed Services University of the Health Sciences · US

Funding

ER-to-Golgi traffic and signal regulation of GPCRsR01GM076167 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WU, GUANGYU · 2006 to 2013
$2.2M
TRENDS IN TRANS-FATTY ACID INTAKE BETWEEN 1980 AND 1997R03HL064592 · NHLBI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HARNACK, LISA · 2000 to 2001
$142k
NHLBI NIH HHS HL64592NIGMS NIH HHS GM76167NIGMS NIH HHS R01 GM076167
6 · The paper itself

Abstract

The physiological function of angiotensin II (Ang II) is mediated through the Ang II type 1 (AT1R) and type 2 (AT2R) receptors. Our previous studies have demonstrated that cell surface targeting of AT1R is regulated by Rab and Sar1 GTPases and the F(x)(6)LL motif in the membrane-proximal C terminus. However, the molecular mechanisms underlying the export of nascent AT2R remain poorly defined. In this report, we determined the role of Rab1 GTPase, which specifically controls protein transport from the endoplasmic reticulum (ER) to the Golgi, and receptor dimerization in the biosynthesis of AT2R. Cell surface expression of AT2R was augmented by transient expression of Rab1 and attenuated by dominant-negative Rab1 mutants and small interfering RNA-mediated knockdown of Rab1. Consistently, AT2R inhibition of epidermal growth factor-activated extracellular signal-regulated kinase 1/2 was significantly reduced by the Rab1 mutants, indicating that endogenous Rab1 modulates the cell surface targeting and signaling of AT2R. It is of interest to note that Rab1 augmented the overall expression of AT2R and its mRNA, whereas the Rab1 mutants attenuated the total AT2R expression and enhanced ubiquitin-dependent AT2R degradation. Furthermore, our previously characterized ER export-deficient AT1R mutant in which the F(x)(6)LL motif was mutated formed both homodimers and heterodimers with AT2R. Dimerization of the AT1R mutant with AT2R blocked AT2R trafficking to the cell surface, suggesting constitutive dimerization of both receptors in the ER and an important role of dimerization in ER export of the receptors. These data demonstrate for the first time that Rab1 GTPase and dimerization modulate export traffic from the ER to the cell surface of newly synthesized AT2R.

Indexed as

Cell LineGene Expression Regulation, EnzymologicHumansMembrane ProteinsProtein Multimerizationrab1 GTP-Binding ProteinsReceptor, Angiotensin, Type 2Membrane Proteinsrab1 GTP-Binding ProteinsReceptor, Angiotensin, Type 2

Identifiers

PMID19357319
PMCPMC2700163
OpenAlexW2133472934

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.