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Nuclear localization and regulation of erk- and rsk-encoded protein kinases.
Open accessAbstract
We demonstrate that members of the erk-encoded family of mitogen-activated protein (MAP) kinases (pp44/42mapk/erk) and members of the rsk-encoded protein kinases (RSKs or pp90rsk) are present in the cytoplasm and nucleus of HeLa cells. Addition of growth factors to serum-deprived cells results in increased tyrosine and threonine phosphorylation and in the activation of cytosolic and nuclear MAP kinases. Activated MAP kinases then phosphorylate (serine/threonine) and activate RSKs. Concurrently, a fraction of the activated MAP kinases and RSKs enter the nucleus. In addition, a distinct growth-regulated RSK-kinase activity (an enzyme[s] that phosphorylates recombinant RSK in vitro and that may be another member of the erk-encoded family of MAP kinases) was found associated with a postnuclear membrane fraction. Regulation of nuclear MAP kinase and RSK activities by growth factors and phorbol ester is coordinate with immediate-early gene expression. Indeed, in vitro, MAP kinase and/or RSK phosphorylates histone H3 and the recombinant c-Fos and c-Jun polypeptides, transcription factors phosphorylated in a variety of cells in response to growth stimuli. These in vitro studies raise the possibility that the MAP kinase/RSK signal transduction pathway represents a protein-Tyr/Ser/Thr phosphorylation cascade with the spatial distribution and temporal regulation that can account for the rapid transmission of growth-regulating information from the membrane, through the cytoplasm, and to the nucleus.
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Metadata
- Authors
- Chen, R. H., Sarnecki, C., & Blenis, J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1992-03
- Volume
- 12
- Issue
- 3
- Pages
- 915-927
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W1821277660
- Cited by
- 1,091
- References
- 1
- FWCI
- 28.12
- Type
- journal article
- Language
- en
- Open access
- green
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