Protein Kinase D and G Subunits Mediate Agonist-evoked Translocation of Protease-activated Receptor-2 from the Golgi Apparatus to the Plasma Membrane
Dane D Jensen, Peishen Zhao, Nestor N Jimenez-Vargas, TinaMarie Lieu, Marina Gerges, Holly R Yeatman, Meritxell Canals, Stephen J Vanner, Daniel P Poole, Nigel W Bunnett
JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2016
Agonist-evoked endocytosis of G protein-coupled receptors has been extensively studied. The mechanisms by which agonists stimulate mobilization and plasma membrane translocation of G protein-coupled receptors from intracellular stores are unexplored. Protease-activated receptor-2 (PAR2) traffics to lysosomes, and sustained protease signaling requires mobilization and plasma membrane trafficking of PAR2 from Golgi stores. We evaluated the contribution of protein kinase D (PKD) and Gβγ to this process. In HEK293 and KNRK cells, the PAR2 agonists trypsin and 2-furoyl-LIGRLO-NH2 activated PKD in the Golgi apparatus, where PKD regulates protein trafficking. PAR2 activation induced translocation o..View full abstract
This work was supported by the National Health and Medical Research Council, The Australian Research Council, and Monash University. Research in the authors' laboratory was funded in part by Takeda Pharmaceuticals, Inc.