Mechanism and Regulation of ERK2 Subcellular Localization

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Mechanism and Regulation of ERK2 Subcellular Localization

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dc.contributor.advisor Cobb, Melanie H. en
dc.creator Whitehurst, Angelique Wright en
dc.date.accessioned 2010-07-12T19:03:13Z en
dc.date.available 2010-07-12T19:03:13Z en
dc.date.issued 2004-05-04 en
dc.identifier.other 59006402 en
dc.identifier.uri http://hdl.handle.net/2152.5/783 en
dc.description.abstract Dynamic changes in the localization of activated proteins can be obligatory events in signaling networks that control cell behavior. ERK1/2 activation contributes to regulated processes such as proliferation, differentiation and survival through the phosphorylation of multiple nuclear and cytoplasmic substrates. The pleiotropic effects of ERK1/2 activation suggest that regulated compartmentalization of the kinases and substrates may contribute to the fidelity of phenotypic changes in response to specific cell stimuli. Therefore, elucidating the mechanism of translocation as well as how this process is controlled is important for understanding how MAP kinases transmit signals. In vitro studies using a permeabilized cell system indicate that nuclear import of ERK2 is not regulated by soluble transport factors, but requires access to nucleoporins. While this process is not influenced by classical import machinery, it can be modulated by anchoring proteins that bind to ERK2 and sequester the kinase in the cytoplasm. One of these proteins, PEA-15, prevents ERK2 import in an in vitro system by inhibiting the kinases' ability to interact with nucleoporins. In vivo assays of phosphorylated ERK1/2 show discrete subcellular localization patterns in response to different stimuli that are independent of the level of ERK1/2 activation. Under conditions in which ERK1/2 is concentrated in the cytoplasm, the nuclear substrate of the kinase, c-Fos, is not expressed, while the cytoplasmic substrate of ERK1/2, p90RSK, is phosphorylated. en
dc.format.medium Electronic en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.subject MAP Kinase Kinase Kinases en
dc.subject Cell Physiological Processes en
dc.subject Phosphorylation en
dc.title Mechanism and Regulation of ERK2 Subcellular Localization en
dc.type.material Text en
dc.type.genre dissertation en
dc.format.digitalOrigin born digital en
thesis.degree.grantor Graduate School of Biomedical Sciences en
thesis.degree.department en
thesis.degree.name Doctor of Philosophy en
thesis.degree.level Ph.D. en
thesis.degree.discipline Cell Regulation en
thesis.date.available 2004-05-04 en

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