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- Title
The C-terminal of the α1b-adreneroceptor is a key determinant for its structure integrity and biological functions.
- Authors
Liu, Ying; Shao, Yu-Ting; Ward, Richard; Ma, Li; Gui, Hao-Xin; Hao, Qian; Mu, Xi; Yang, Yang; An, Su; Guo, Xiao-Xi; Xu, Tian-Rui
- Abstract
The C-terminal of G protein-coupled receptors is now recognized as being important for G protein activation and signaling function. To detect the role of C-terminal tail in receptor activation, we used the α1b-AR, which has a long C-terminal of 164 amino acids. We constructed the intramolecular FRET sensors, in which the C-terminal was truncated to 10 (∆C-10), 20 (∆C-20), 30 (∆C-30), 50 (∆C-50), 70 (∆C-70), or 90 (∆C-90). The truncated mutants of ∆C-10, ∆C-20, or ∆C-30 cannot induce FRET signal changes and downstream ERK1/2 phosphorylation. However, the truncated mutants of ∆C-50, ∆C-70, or ∆C-90 induce significant FRET signal changes and downstream ERK1/2 phosphorylation, especially ∆C-90. This is particularly true in the case of the ∆C-90, ∆C-70, or ∆C-50 which retained the potential phosphorylation sites (Ser401, Ser404, Ser408, or Ser410). The ∆C-90 showed an increase in agonist-induced FRET signal changes and ERK1/2 phosphorylation in PKC- or endocytosis-dependent and EGFR-, src-, or β-arrestin2-independent.
- Subjects
MORPHOLOGY; G proteins; G protein coupled receptors
- Publication
Bioscience, Biotechnology & Biochemistry, 2021, Vol 85, Issue 5, p1128
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1093/bbb/zbab034