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• W2116918105 abstract "In resting cells NF-κB transcription factors are retained in the cytoplasm as latent inactive complexes, until they are activated and rapidly transported into the nucleus. We show that all NF-κB proteins are imported into the nucleus via a subset of importin α isoforms. Our data indicate that the NF-κB components of the classical and alternative pathways have somewhat different specifities to importin α molecules. Based on the results from binding experiments of in vitro-translated and Sendai virus infection-induced or TNF-α-stimulated endogenous NF-κB proteins, it can be predicted that the specifity of NF-κB proteins to importin α molecules is different and changes upon the composition of the imported dimer. p52 protein binds directly to importin α3, α4, α5 and α6 and c-Rel binds to importin α5, α6 and α7 via a previously described monopartite nuclear localization signals (NLSs). Here we show that RelB, instead, has a bipartite arginine/lysine-rich NLS that mediates the binding of RelB to importin α5 and α6 and subsequent nuclear translocation of the protein. Moreover, we show that the nuclear import of p52/RelB heterodimers is mediated exclusively by the NLS of RelB. In addition, we found that the NLS of p52 mediates the nuclear import of p52/p65 heterodimers." @default.
• W2116918105 created "2016-06-24" @default.
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• W2116918105 date "2008-08-01" @default.
• W2116918105 modified "2023-09-30" @default.
• W2116918105 title "NF-κB p52, RelB and c-Rel are transported into the nucleus via a subset of importin α molecules" @default.
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• W2116918105 doi "https://doi.org/10.1016/j.cellsig.2008.03.012" @default.
• W2116918105 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18462924" @default.
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