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Mol. Cells 2009; 28(1): 25-30

Published online July 31, 2009

https://doi.org/10.1007/s10059-009-0104-1

© The Korean Society for Molecular and Cellular Biology

A Protein Tyrosine Phosphatase Inhibitor,Pervanadate, Inhibits Angiotensin II-Induced-Arrestin Cleavage

Sei-Heon Jang, Si Ae Hwang, Mijin Kim, Sung-Hae Yun, Moon-Sook Kim, Sadashiva S. Karnik, and ChangWoo Lee

Received: March 8, 2009; Revised: May 20, 2009; Accepted: June 9, 2009

Abstract

β-Arrestins turn off G protein-mediated signals and initi-ate distinct G protein-independent signaling pathways. We previously demonstrated that angiotensin AT1 receptor-bound β-arrestin 1 is cleaved after Phe388 upon angiotensin II stimulation. The mechanism and signaling pathway of angiotensin II-induced β-arrestin cleavage remain largely unknown. Here, we show that protein Tyr phosphatase activity is involved in the regulation of β-arrestin 1 cleavage. Tagging of green fluorescent protein (GFP) either to the N-terminus or C-terminus of β-arrestin 1 induced conformational changes and the cleavage of β-arrestin 1 without angiotensin AT1 receptor activation. Orthovanadate and molybdate, inhibitors of protein Tyr phosphatase, attenuated the cleavage of C-terminal GFP-tagged β-arrestin 1 in vitro. The inhibitory effects of okadaic acid and pyrophosphate, which are inhibitors of protein Ser/Thr phosphatase, were less than those of protein Tyr phosphatase inhibitors. Cell-permeable pervanadate inhibited angiotensin II-induced cleavage of β-arrestin 1 in COS-1 cells. Our findings suggest that Tyr phosphorylation signaling is involved in the regulation of angiotensin II-induced β-arrestin cleavage.

Keywords β-arrestin, angiotensin AT1 receptor, orthovanadate, pervanadate, protein tyrosine phosphatase

Article

Research Article

Mol. Cells 2009; 28(1): 25-30

Published online July 31, 2009 https://doi.org/10.1007/s10059-009-0104-1

Copyright © The Korean Society for Molecular and Cellular Biology.

A Protein Tyrosine Phosphatase Inhibitor,Pervanadate, Inhibits Angiotensin II-Induced-Arrestin Cleavage

Sei-Heon Jang, Si Ae Hwang, Mijin Kim, Sung-Hae Yun, Moon-Sook Kim, Sadashiva S. Karnik, and ChangWoo Lee

Received: March 8, 2009; Revised: May 20, 2009; Accepted: June 9, 2009

Abstract

β-Arrestins turn off G protein-mediated signals and initi-ate distinct G protein-independent signaling pathways. We previously demonstrated that angiotensin AT1 receptor-bound β-arrestin 1 is cleaved after Phe388 upon angiotensin II stimulation. The mechanism and signaling pathway of angiotensin II-induced β-arrestin cleavage remain largely unknown. Here, we show that protein Tyr phosphatase activity is involved in the regulation of β-arrestin 1 cleavage. Tagging of green fluorescent protein (GFP) either to the N-terminus or C-terminus of β-arrestin 1 induced conformational changes and the cleavage of β-arrestin 1 without angiotensin AT1 receptor activation. Orthovanadate and molybdate, inhibitors of protein Tyr phosphatase, attenuated the cleavage of C-terminal GFP-tagged β-arrestin 1 in vitro. The inhibitory effects of okadaic acid and pyrophosphate, which are inhibitors of protein Ser/Thr phosphatase, were less than those of protein Tyr phosphatase inhibitors. Cell-permeable pervanadate inhibited angiotensin II-induced cleavage of β-arrestin 1 in COS-1 cells. Our findings suggest that Tyr phosphorylation signaling is involved in the regulation of angiotensin II-induced β-arrestin cleavage.

Keywords: β,-arrestin, angiotensin AT1 receptor, orthovanadate, pervanadate, protein tyrosine phosphatase

Mol. Cells
Sep 30, 2022 Vol.45 No.9, pp. 603~672
COVER PICTURE
The Target of Rapamycin Complex (TORC) is a central regulatory hub in eukaryotes, which is well conserved in diverse plant species, including tomato (Solanum lycopersicum). Inhibition of TORC genes (SlTOR, SlLST8, and SlRAPTOR) by VIGS (virus-induced gene silencing) results in early fruit ripening in tomato. The red/ orange tomatoes are early-ripened TORC-silenced fruits, while the green tomato is a control fruit. Top, left, control fruit (TRV2-myc); top, right, TRV2-SlLST8; bottom, left, TRV2-SlTOR; bottom, right, TRV2-SlRAPTOR(Choi et al., pp. 660-672).

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