Cytoplasmic localization of the mitogen-activated protein kinase activator MEK.
作者： Chao-Feng Zheng , Kun-Liang Guan , None
DOI: 10.1016/S0021-9258(17)32112-9
关键词: Activator (genetics) 、 Mitogen-activated protein kinase kinase 、 MAPK/ERK pathway 、 Mitogen-activated protein kinase 、 Molecular biology 、 Kinase 、 Biology 、 Protein kinase A 、 Cell biology 、 Cytoplasm 、 Signal transduction
摘要: The mitogen-activated protein kinase (MAPK) or extracellular signal-regulated (ERK) is phosphorylated and activated by an upstream activator kinase, MEK (MAPK ERK kinase), in response to mitogenic growth factors. ERKs translocate into the nucleus upon mitogen stimulation, suggesting that subcellular redistribution of may play a critical role signal transfer from cytoplasm nucleus. We demonstrated this report was exclusively localized several cell lines, including Swiss 3T3, HeLa, COS, PC12. Immunofluorescence analysis both native transiently expressed with MEK-specific antibody revealed MEK1 MEK2 were only cytoplasm. cytoplasmic localization further supported fractionations as well detergent permeabilization experiments. In contrast ERK, stimulation did not cause any nuclear accumulation MEK. These data suggest could subsequently phosphorylate its substrates.
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