TAILIEUCHUNG - Báo cáo khoa học: Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN

The Per-Arnt-Sim (PAS) domain serine⁄threonine kinase PASKIN, or PAS kinase, links energy flux and protein synthesis in yeast, regulates glycogen synthesis and protein translation in mammals, and might be involved in insulin regulation in the pancreas. | IFEBS Journal Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN Philipp Schlafli Juliane Troger f Katrin EckhardtỊ Emanuela Borter Patrick Spielmann and Roland H. Wenger Institute of Physiology and Zurich Center for Integrative Human Physiology University of Zurich Switzerland Keywords metabolism phospholipid protein translation ribosomalprotein S6 sensory kinase Correspondence R. H. Wenger Institute of Physiology University of Zurich Winterthurerstrasse 190 CH-8057 Zurich Switzerland Fax 41 0 44 6356814 Tel 41 0 44 6355065 E-mail Website http These authors contributed equally to this work Present addresses fDivision of Digestive and Liver Diseases Department of Medicine Columbia University New York NY USA tInstitute of CellBiology ETH Zurich Switzerland Biogen-Dompe Zug Switzerland Received 25 October 2010 accepted 14 March 2011 doi The Per-Arnt-Sim PAS domain serine threonine kinase PASKIN or PAS kinase links energy flux and protein synthesis in yeast regulates glycogen synthesis and protein translation in mammals and might be involved in insulin regulation in the pancreas. According to the current model binding of a putative ligand to the PAS domain disinhibits the kinase domain leading to PASKIN autophosphorylation and increased kinase activity. To date only synthetic but no endogenous PASKIN ligands have been reported. In the present study we identified a number of novel PASKIN kinase targets including ribosomal protein S6. Together with our previous identification of eukaryotic elongation factor 1A1 this suggests a role for PASKIN in the regulation of mammalian protein translation. When searching for endogenous PASKIN ligands we found that various phospholipids can bind PASKIN and stimulate its autophosphorylation. Interestingly the strongest binding and autophosphorylation was achieved with .

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