Ezrin, radixin, and moesin phosphorylation in NIH3T3 cells revealed angiotensin II type 1 receptor cell-type-dependent biased signaling

Islam A.A.E.H. Ibrahim, Nakaya Michio, Hitoshi Kurose

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

β-Arrestin-biased agonists are a new class of drugs with promising therapeutic effects. The molecular mechanisms of β-arrestin-biased agonists are still not completely identified. Here, we investigated the effect of angiotensin II (AngII) and [Sar1,Ile4,Ile8] AngII (SII), a β-arrestin- biased agonist, on ezrin-radixin-moesin (ERM) phosphorylation in NIH3T3 cells (a fibroblast cell line) stably expressing AngII type 1A receptor. ERM proteins are cross-linkers between the plasma membrane and the actin cytoskeleton and control a number of signaling pathways. We also investigated the role of Gαq protein and β-arrestins in mediating ERM phosphorylation. We found that AngII stimulates ERM phosphorylation by acting as a β-arrestin-biased agonist and AngII-stimulated ERM phosphorylation is mediated by β-arrestin2 not β-arrestin1. We also found that SII inhibits ERM phosphorylation by acting as a Gαq protein-biased agonist. We concluded that ERM phosphorylation is a unique β-arrestin-biased agonism signal. Both AngII and SII can activate either Gαq protein or β-arrestin-mediated signaling as functional biased agonists according to the type of the cell on which they act.

Original languageEnglish
Pages (from-to)1-9
Number of pages9
JournalJournal of Pharmacological Sciences
Volume122
Issue number1
DOIs
Publication statusPublished - May 29 2013

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Pharmacology

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