the role of palmitoylation in signalling, cellular trafficking and plasma membrane localization of protease-activated receptor-2棕榈酰化在信号的作用,细胞贩运和质膜定位protease-activated受体2.pdfVIP
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the role of palmitoylation in signalling, cellular trafficking and plasma membrane localization of protease-activated receptor-2棕榈酰化在信号的作用,细胞贩运和质膜定位protease-activated受体2
The Role of Palmitoylation in Signalling, Cellular
Trafficking and Plasma Membrane Localization of
Protease-Activated Receptor-2
1,2 1 1 1 1
Mark N. Adams , Melinda E. Christensen , Yaowu He , Nigel J. Waterhouse , John D. Hooper *
1 Mater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland, Australia, 2 Institute of Health and Biomedical Innovation, Queensland
University of Technology, Kelvin Grove, Queensland, Australia
Abstract
Protease-activated receptor-2 (PAR2) is a G protein coupled receptor (GPCR) activated by proteolytic cleavage of its amino
terminal domain by trypsin-like serine proteases. This irreversible activation mechanism leads to rapid receptor
desensitization by internalisation and degradation. We have explored the role of palmitoylation, the post-translational
addition of palmitate, in PAR2 signalling, trafficking, cell surface expression and desensitization. Experiments using the
palmitoylation inhibitor 2-bromopalmitate indicated that palmitate addition is important in trafficking of PAR2
endogenously expressed by prostate cancer cell lines. This was supported by palmitate labelling using two approaches,
which showed that PAR2 stably expressed by CHO-K1 cells is palmitoylated and that palmitoylation occurs on cysteine 361.
Palmitoylation is required for optimal PAR2 signalling as Ca2+ flux assays indicated that in response to trypsin agonism,
palmitoylation deficient PAR2 is ,9 fold less potent than wildtype receptor with a reduction of about 33% in the maximum
signal induced via the mutant receptor. Confocal microscopy, flow cyt
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