Localization and trafficking of fluorescently tagged ERK1 and ERK2.
The action of ERK1 and ERK2 activity on the nuclear substrates requires crossing the nuclear envelope and the localization of phospho-ERK into the nucleus. The nucleo-cytoplasmic trafficking of ERK is therefore crucial for the correct functioning of the pathway. Indeed, this step is necessary for the correct control of gene expression by growth-factors, for morphological transformation of fibroblasts and for neurite extension in PC12. Furthermore, disruption of ERK2 localization in the nucleus severely affects the transduction of ERK2 signaling. This process has now been observed and quantitatively measured by expressing fluorescently tagged ERK1 and ERK2. These experiments provide important insight on the operation of these signaling modules and have revealed an hitherto unknown functional difference between ERK1 and ERK2.
Marchi
Matilde
M
NEST/INFM and Scuola Normale Superiore, Pisa, Italy.
Parra
Riccardo
R
Costa
Mario
M
Ratto
Gian Michele
GM
D021581:Active Transport, Cell Nucleus; D000818:Animals; D002138:Calibration; D002467:Cell Nucleus / Q000378:metabolism; D002470:Cell Survival; D003593:Cytoplasm / Q000378:metabolism; D036681:Fluorescence Recovery After Photobleaching; D005456:Fluorescent Dyes / Q000378:metabolism*; D051379:Mice; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism*; D048052:Mitogen-Activated Protein Kinase 3 / Q000378:metabolism*; D041681:NIH 3T3 Cells; D021381:Protein Transport; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013997:Time Factors; D014162:Transfection
D005456:Fluorescent Dyes; D011993:Recombinant Fusion Proteins; D019950:Mitogen-Activated Protein Kinase 1; D048052:Mitogen-Activated Protein Kinase 3