Roles of phosphotase 2A in nociceptive signal processing
1 Department of Anesthesiology, Beijing Chaoyang Hospital, Capital Medical University, Beijing 100020, China
2 Department of Neuroscience and Cell Biology, The University of Texas Medical Branch, Galveston, TX 77555-0517, USA
3 Department of Neurosurgery, Cancer Center, Sun Yat-sen University, Guangzhou 510060, China
4 Department of Neurosurgery and Neurology, Lineberger Cancer Center, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA
Molecular Pain 2013, 9:46 doi:10.1186/1744-8069-9-46Published: 8 September 2013
Multiple protein kinases affect the responses of dorsal horn neurons through phosphorylation of synaptic receptors and proteins involved in intracellular signal transduction pathways, and the consequences of this modulation may be spinal central sensitization. In contrast, the phosphatases catalyze an opposing reaction of de-phosphorylation, which may also modulate the functions of crucial proteins in signaling nociception. This is an important mechanism in the regulation of intracellular signal transduction pathways in nociceptive neurons. Accumulated evidence has shown that phosphatase 2A (PP2A), a serine/threonine specific phosphatase, is implicated in synaptic plasticity of the central nervous system and central sensitization of nociception. Therefore, targeting protein phosphotase 2A may provide an effective and novel strategy for the treatment of clinical pain. This review will characterize the structure and functional regulation of neuronal PP2A and bring together recent advances on the modulation of PP2A in targeted downstream substrates and relevant multiple nociceptive signaling molecules.