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• W1966604359 abstract "Insulin receptor substrates (IRSs) play essential roles in signal transduction of insulin and insulin-like growth factors. Previously, we showed that IRS-3 is localized to the nucleus as well as the cytosol, while IRS-1 and 2 are mainly localized to the cytoplasm. In the present study, we found that importin beta directly interacts with IRS-3 and is able to mediate nuclear transport of IRS-3. Importin beta interacted with the pleckstrin homology domain, the phosphotyrosine binding domain and the C-terminal region of IRS-3; indeed all of these fragments exhibited predominant nuclear localization. By contrast, almost no interaction of importin beta with IRS-1 and -2 was observed, and their C-terminal regions displayed discrete spotty images in the cytosol. In addition, using chimeric proteins between IRS-1 and IRS-3, we revealed that the C-terminal regions are the main determinants of the differing subcellular localizations of IRS-1 and IRS-3." @default.
• W1966604359 created "2016-06-24" @default.
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• W1966604359 date "2008-12-01" @default.
• W1966604359 modified "2023-10-14" @default.
• W1966604359 title "Differential subcellular localization of insulin receptor substrates depends on C-terminal regions and importin β" @default.
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• W1966604359 doi "https://doi.org/10.1016/j.bbrc.2008.09.106" @default.
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