α1A-Adrenergic Receptor Induces Activation of Extracellular Signal-Regulated Kinase 1/2 through Endocytic Pathway

• DOI: 10.1371/journal.pone.0021520
• Publication Date: 2011-06-28T21:01:08Z
• Authors: Fei Liu; Kangmin He; Xinxing Yang; Ning Xu; Zhangyi Liang; Ming Xu; Xinsheng Zhao; Qide Han; Youyi Zhang
• Keywords: Cytochalasin D; HEK 293 cells

G protein-coupled receptors (GPCRs) activate mitogen-activated protein kinases through a number of distinct pathways in cells. Increasing evidence has suggested that endosomal signaling an important role receptor signal transduction. Here we investigated the involvement endocytosis α(1A)-adrenergic (α(1A)-AR)-induced activation extracellular signal-regulated kinase 1/2 (ERK1/2). Agonist-mediated endocytic traffic α(1A)-AR was assessed by real-time imaging living, stably transfected human embryonic kidney 293A cells (HEK-293A). internalized dynamically with agonist stimulation, and actin filaments regulated initial trafficking α(1A)-AR. α(1A)-AR-induced ERK1/2 but not p38 MAPK sensitive to disruption endocytosis, as demonstrated 4°C chilling, dynamin mutation treatment cytochalasin D (actin depolymerizing agent). Activation C (PKC) C-Raf affected chilling or treatment. U73122 (a phospholipase [PLC] inhibitor) Ro 31-8220 PKC inhibited α(1B)-AR- activation. These data suggest pathway is involved activation, which independent G(q)/PLC/PKC signaling.