Evidence map›Paper›PMID 26703465›Full record

ArticleThe Journal of biological chemistry2016

β-Arrestin-mediated Angiotensin II Signaling Controls the Activation of ARF6 Protein and Endocytosis in Migration of Vascular Smooth Muscle Cells.

Ricardo Charles, Yoon Namkung, Mathieu Cotton, Stéphane A Laporte, Audrey Claing

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Insights Into the Role of Angiotensin-II ATHypertension (Dallas, Tex. : 1979) · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    Review
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  12. Review
  13. Article
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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 2 institutions in 1 country.

Ricardo CharlesFrom the Department of Pharmacology, Faculty of Medicine, Université de Montréal, Montreal, Quebec H3C 3J7 and.
Yoon Namkungthe Department of Medicine, Research Institute of McGill University Health Center, McGill University, Montreal, Quebec H4A 3J1, Canada.
Mathieu CottonFrom the Department of Pharmacology, Faculty of Medicine, Université de Montréal, Montreal, Quebec H3C 3J7 and.
Stéphane A Laportethe Department of Medicine, Research Institute of McGill University Health Center, McGill University, Montreal, Quebec H4A 3J1, Canada.
Audrey ClaingFrom the Department of Pharmacology, Faculty of Medicine, Université de Montréal, Montreal, Quebec H3C 3J7 and audrey.claing@umontreal.ca.
Université de Montréal · CAMcGill University · CA

Funding

Canadian Institutes of Health Research MOP-74603Canadian Institutes of Health Research MOP-79470
6 · The paper itself

Abstract

Angiotensin II (Ang II) is a vasopressive hormone but is also a potent activator of cellular migration. We have previously shown that it can promote the activation of the GTPase ARF6 in a heterologous overexpressing system. The molecular mechanisms by which receptors control the activation of this small G protein remain, however, largely unknown. Furthermore, how ARF6 coordinates the activation of complex cellular responses needs to be further elucidated. In this study, we demonstrate that Ang II receptors engage β-arrestin, but not Gq, to mediate ARF6 activation in HEK 293 cells. To further confirm the key role of β-arrestin proteins, we overexpressed β-arrestin2-(1-320), a dominant negative mutant known to block receptor endocytosis. We show that expression of this truncated construct does not support the activation of the GTPase nor cell migration. Interestingly, β-arrestin2 can interact with the ARF guanine nucleotide exchange factor ARNO, although the C-terminally lacking mutant does not. We finally examined whether receptor endocytosis controlled ARF6 activation and cell migration. Although the clathrin inhibitor PitStop2 did not impact the ability of Ang II to activate ARF6, cell migration was markedly impaired. To further show that ARF activation regulates key signaling events leading to migration, we also examined MAPK activation. We demonstrate that this signaling axis is relevant in smooth muscle cells of the vasculature. Altogether, our findings show for the first time that Ang II receptor signaling to β-arrestin regulates ARF6 activation. These proteins together control receptor endocytosis and ultimately cell migration.

Indexed as

ADP-Ribosylation Factor 6ADP-Ribosylation FactorsAngiotensin IIAnimalsArrestinsbeta-ArrestinsCell MovementEndocytosisEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHEK293 CellsHumansMAP Kinase Signaling SystemMuscle, Smooth, VascularMyocytes, Smooth MuscleRatsADP-Ribosylation Factor 6ADP-Ribosylation FactorsAngiotensin IIARF6 protein, humanArf6 protein, ratArrestinsbeta-ArrestinsExtracellular Signal-Regulated MAP Kinasespitstop 2Receptors, AngiotensinSulfonamidesThiazolidines7-helix receptorADP ribosylation factor (ARF)angiotensin IIarrestincell migrationvascular smooth muscle cells

Identifiers

PMID26703465
PMCPMC4759175
OpenAlexW2206930456

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.