Journal
FRONTIERS IN BIOSCIENCE-LANDMARK
Volume 11, Issue -, Pages 2714-2724Publisher
FRONTIERS IN BIOSCIENCE INC
DOI: 10.2741/2001
Keywords
kinase; DUSP18; SAPK; JNK; phosphorylation; interaction
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The SAPK/JNKs play important roles in numerous cellular processes, and for this reason they have become putative drug targets. Most dual-specificity protein phosphatases (DSPs) play important roles in the regulation of mitogenic signal transduction and cell cycle control in response to extracellular stimuli. Dual-specificity phosphatase 18 (DUSP18), a newly recognized SAPK/JNK phosphatase, is widely expressed. This expression is modulated in response to extracelluar stimuli. By phosphorylation assay, pull down and coimmunoprecipetation experiments, it is shown here that DUSP18 interacts with SAPK/JNK and dephosphorylates it both in vitro and in vivo. DUSP18 does not dephosphorylate p38 or p44ERK1. Furthermore, DUSP18 inhibits SAPK/JNK pathway in vivo. Based on these findings, DUSP18 appears to serve an important role by regulation of SAPK/JNK pathway.
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