PMID- 23575451
OWN - NLM
STAT- MEDLINE
DCOM- 20131206
LR  - 20190911
IS  - 1347-8648 (Electronic)
IS  - 1347-8613 (Linking)
VI  - 122
IP  - 1
DP  - 2013
TI  - Ezrin, radixin, and moesin phosphorylation in NIH3T3 cells revealed angiotensin 
      II type 1 receptor cell-type-dependent biased signaling.
PG  - 1-9
AB  - beta-Arrestin-biased agonists are a new class of drugs with promising therapeutic 
      effects. The molecular mechanisms of beta-arrestin-biased agonists are still not 
      completely identified. Here, we investigated the effect of angiotensin II (AngII) 
      and [Sar1,Ile4,Ile8] AngII (SII), a beta-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 Galphaq protein and beta-arrestins 
      in mediating ERM phosphorylation. We found that AngII stimulates ERM 
      phosphorylation by acting as a beta-arrestin-biased agonist and AngII-stimulated ERM 
      phosphorylation is mediated by beta-arrestin2 not beta-arrestin1. We also found that 
      SII inhibits ERM phosphorylation by acting as a Galphaq protein-biased agonist. We 
      concluded that ERM phosphorylation is a unique beta-arrestin-biased agonism signal. 
      Both AngII and SII can activate either Galphaq protein or beta-arrestin-mediated 
      signaling as functional biased agonists according to the type of the cell on 
      which they act.
FAU - Ibrahim, Islam A A E-H
AU  - Ibrahim IA
AD  - Department of Pharmacology and Toxicology, Graduate School of Pharmaceutical 
      Sciences, Kyushu University, Japan.
FAU - Nakaya, Michio
AU  - Nakaya M
FAU - Kurose, Hitoshi
AU  - Kurose H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130409
PL  - Japan
TA  - J Pharmacol Sci
JT  - Journal of pharmacological sciences
JID - 101167001
RN  - 0 (Arrestins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Receptor, Angiotensin, Type 1)
RN  - 0 (beta-Arrestins)
RN  - 0 (ezrin)
RN  - 11128-99-7 (Angiotensin II)
RN  - 144131-77-1 (moesin)
RN  - 144517-21-5 (radixin)
RN  - EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11)
SB  - IM
MH  - Angiotensin II/*pharmacology
MH  - Animals
MH  - Arrestins/metabolism
MH  - Cytoskeletal Proteins/*metabolism
MH  - GTP-Binding Protein alpha Subunits, Gq-G11/metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Microfilament Proteins/*metabolism
MH  - NIH 3T3 Cells
MH  - Phosphorylation
MH  - Receptor, Angiotensin, Type 1/agonists/*metabolism
MH  - Signal Transduction
MH  - beta-Arrestins
EDAT- 2013/04/12 06:00
MHDA- 2013/12/16 06:00
CRDT- 2013/04/12 06:00
PHST- 2013/04/12 06:00 [entrez]
PHST- 2013/04/12 06:00 [pubmed]
PHST- 2013/12/16 06:00 [medline]
AID - DN/JST.JSTAGE/jphs/12288FP [pii]
AID - 10.1254/jphs.12288fp [doi]
PST - ppublish
SO  - J Pharmacol Sci. 2013;122(1):1-9. doi: 10.1254/jphs.12288fp. Epub 2013 Apr 9.