ERK Nuclear Translocation Is Dimerization-independent but Controlled by the Rate of Phosphorylation

• Published in: The Journal of biological chemistry Vol. 285; no. 5; pp. 3092 - 3102
• Main Authors: Lidke, Diane S., Huang, Fang, Post, Janine N., Rieger, Bernd, Wilsbacher, Julie, Thomas, James L., Pouysségur, Jacques, Jovin, Thomas M., Lenormand, Philippe
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.01.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Active Transport, Cell Nucleus; Animals; Biochemistry, Molecular Biology; Cell Nucleus - metabolism; Cell/Compartmentation; Cytoplasm - metabolism; Dimerization; DNA, Complementary - metabolism; Enzymes/Kinase; Extracellular Signal-Regulated MAP Kinases - metabolism; Green Fluorescent Proteins - metabolism; Humans; Life Sciences; Mechanisms of Signal Transduction; Methods/Fluorescence; Mice; Mice, Knockout; Microscopy, Confocal - methods; Microscopy, Fluorescence - methods; Models, Biological; Nucleus/Nuclear Import; Phosphorylation; Protein/Nuclear Translocation; Signal Transduction/Protein Kinases/MAP; Enzymes/Kinase; Phosphorylation; Signal Transduction/Protein Kinases/MAP; Cell/Compartmentation; Protein/Nuclear Translocation; Methods/Fluorescence; Nucleus/Nuclear Import

Upon activation, ERKs translocate from the cytoplasm to the nucleus. This process is required for the induction of many cellular responses, yet the molecular mechanisms that regulate ERK nuclear translocation are not fully understood. We have used a mouse embryo fibroblast ERK1-knock-out cell line e...