Phosphorylation of RACK1 in plants
31 August 2015, Plant Signaling and Behavior 10(8): e1022013; doi: 10.1080/15592324.2015.1022013
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.
(2015) Phosphorylation of RACK1 in plants, Plant Signaling & Behavior, 10:8,