title: Phosphorylation of RACK1 in plants.
abstract: Receptor for Activated C Kinase 1 (RACK1) is a versatile scaffold protein that interacts with a large, diverse group of proteins to regulate various signaling cascades. RACK1 has been shown to regulate hormonal signaling, stress responses and multiple processes of growth and development in plants. However, little is known about the molecular mechanism underlying these regulations. Recently, it has been demonstrated that Arabidopsis RACK1 is phosphorylated by an atypical serine/threonine protein kinase, WITH NO LYSINE 8 (WNK8). Furthermore, RACK1 phosphorylation by WNK8 negatively regulates RACK1 function by influencing its protein stability. These findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.
authors: a Biosciences Division; Oak Ridge National Laboratory ; Oak Ridge , TN USA.
authors: Jin-Gui
authors: JG
authors: Chen
mesh_terms: D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D059748:Proteolysis; D000075370:Receptors for Activated C Kinase; D011956:Receptors, Cell Surface / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; C515163:RACK1 protein, Arabidopsis; D000075370:Receptors for Activated C Kinase; D011956:Receptors, Cell Surface; D017346:Protein Serine-Threonine Kinases; C508913:WNK8 protein, Arabidopsis
keywords: Arabidopsis; RACK1; WNK8; kinase; phosphorylation; protein degradation; scaffold protein