期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 17, 页码 -出版社
MDPI
DOI: 10.3390/ijms21176102
关键词
p38MAPK; nuclear translocation; beta-like importins; inflammation; cancer
The p38 mitogen-activated protein kinase (p38MAPK, termed here p38) cascade is a central signaling pathway that transmits stress and other signals to various intracellular targets in the cytoplasm and nucleus. More than 150 substrates of p38 alpha/beta have been identified, and this number is likely to increase. The phosphorylation of these substrates initiates or regulates a large number of cellular processes including transcription, translation, RNA processing and cell cycle progression, as well as degradation and the nuclear translocation of various proteins. Being such a central signaling cascade, its dysregulation is associated with many pathologies, particularly inflammation and cancer. One of the hallmarks of p38 alpha/beta signaling is its stimulated nuclear translocation, which occurs shortly after extracellular stimulation. Although p38 alpha/beta do not contain nuclear localization or nuclear export signals, they rapidly and robustly translocate to the nucleus, and they are exported back to the cytoplasm within minutes to hours. Here, we describe the physiological and pathological roles of p38 alpha/beta phosphorylation, concentrating mainly on the ill-reviewed regulation of p38 alpha/beta substrate degradation and nuclear translocation. In addition, we provide information on the p38 alpha/beta 's substrates, concentrating mainly on the nuclear targets and their role in p38 alpha/beta functions. Finally, we also provide information on the mechanisms of nuclear p38 alpha/beta translocation and its use as a therapeutic target for p38 alpha/beta-dependent diseases.
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