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The regulators of G protein signaling RGS 16 and RGS 18 inhibit protease‐activated receptor 2/Gi/o signaling through distinct interactions with Gα in live cells
Author(s) -
Kim Kiman,
Lee Jinyong,
Ghil Sungho
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13220
Subject(s) - microbiology and biotechnology , g protein coupled receptor , g protein , signal transduction , regulator of g protein signaling , proteases , receptor , chemistry , biology , gtpase activating protein , biochemistry , enzyme
Protease‐activated receptor 2 ( PAR 2) is a G protein‐coupled receptor ( GPCR ) activated by endogenous proteases, in particular, trypsin. Although regulators of G protein signaling ( RGS ) are known to inhibit GPCR /Gα‐mediated signaling, their specific effects on PAR 2 are poorly understood at present. Here, we use a bioluminescence resonance energy transfer technique to investigate whether RGS 16 and RGS 18 bind PAR 2 in live cells to regulate PAR 2/Gα i/o ‐mediated signaling. Notably, we find that RGS 16 binds to PAR 2 in the presence of Gα i while RGS 18 does not interact with PAR 2, regardless of the presence of Gα. Both RGS 16 and RGS 18 inhibit PAR 2/Gα i/o ‐mediated signaling. To our knowledge, the current study is the first to highlight the effects of RGS proteins on PAR 2‐mediated signaling.