caa a22 4500 606176632 CHVBK 20210128100748.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00018-014-1775-0 doi (NATIONALLICENCE)springer-10.1007/s00018-014-1775-0 The expansion of GPCR transactivation-dependent signalling to include serine/threonine kinase receptors represents a new cell signalling frontier [Elektronische Daten] [Danielle Kamato, Muhamad Rostam, Rebekah Bernard, Terrence Piva, Nitin Mantri, Daniel Guidone, Wenhua Zheng, Narin Osman, Peter Little] G protein-coupled receptor (GPCR) signalling is mediated through transactivation-independent signalling pathways or the transactivation of protein tyrosine kinase receptors and the recently reported activation of the serine/threonine kinase receptors, most notably the transforming growth factor-β receptor family. Since the original observation of GPCR transactivation of protein tyrosine kinase receptors, there has been considerable work on the mechanism of transactivation and several pathways are prominent. These pathways include the "triple membrane bypass” pathway and the generation of reactive oxygen species. The recent recognition of GPCR transactivation of serine/threonine kinase receptors enormously broadens the GPCR signalling paradigm. It may be predicted that the transactivation of serine/threonine kinase receptors would have mechanistic similarities with transactivation of tyrosine kinase pathways; however, initial studies suggest that these two transactivation pathways are mechanistically distinct. Important questions are the relative importance of tyrosine and serine/threonine transactivation pathways, the contribution of transactivation to overall GPCR signalling, mechanisms of transactivation and the range of cell types in which this phenomenon occurs. The ultimate significance of transactivation-dependent signalling remains to be defined but it appears to be prominent and if so will represent a new cell signalling frontier. Springer Basel, 2014 GPCR nationallicence Transactivation-dependent nationallicence Transactivation-independent nationallicence Cell signalling nationallicence G proteins nationallicence Rho/ROCK nationallicence Kamato Danielle Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Rostam Muhamad Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Bernard Rebekah Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Piva Terrence Discipline of Cell Biology and Anatomy, School of Medical Sciences and Health Innovations Research Institute, 3083, Bundoora, VIC, Australia aut Mantri Nitin School of Applied Sciences, RMIT University, 3083, Bundoora, VIC, Australia aut Guidone Daniel Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Zheng Wenhua State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Centre and School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, People's Republic of China aut Osman Narin Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Little Peter Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut Cellular and Molecular Life Sciences Springer Basel 72/4(2015-02-01), 799-808 1420-682X 72:4<799 2015 72 18 https://doi.org/10.1007/s00018-014-1775-0 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1775-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kamato Danielle Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Rostam Muhamad Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Bernard Rebekah Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Piva Terrence Discipline of Cell Biology and Anatomy, School of Medical Sciences and Health Innovations Research Institute, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Mantri Nitin School of Applied Sciences, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Guidone Daniel Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Zheng Wenhua State Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Centre and School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, People's Republic of China aut NATIONALLICENCE 700 1- Osman Narin Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 700 1- Little Peter Diabetes Complications Laboratory, Discipline of Pharmacy, School of Medical Sciences and Diabetes Complications Group, RMIT University, 3083, Bundoora, VIC, Australia aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/4(2015-02-01), 799-808 1420-682X 72:4<799 2015 72 18