Classical Nuclear Localization Signals: Definition, Function, and Interaction with Importin α*
By A. Lange, Ryan E. Mills, Christoph Lange, M. Stewart, S. Devine, A. Corbett. Journal of Biological Chemistry, 2007
1,191 citations recorded by the source corpus.
The best understood system for the transport of macromolecules between the cytoplasm and the nucleus is the classical nuclear import pathway. In this pathway, a protein containing a classical basic nuclear localization signal (NLS) is imported by a heterodimeric import receptor consisting of the β-karyopherin importin β, which mediates interactions with the nuclear pore complex, and the adaptor protein importin α, which directly binds the classical NLS. Here we review recent studies that have advanced our understanding of this pathway and also take a bioinformatics approach to analyze the likely prevalence of this system in vivo. Finally, we describe how a predicted NLS within a protein of interest can be confirmed experimentally to be functionally important.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c3793f86f9d037c3681341fb9d48a34e49561d18
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Citations in the corpus
- Nanomedicine in cancer therapy (2023, background): “370 It has been shown that NLS-conjugated nanocarriers (NLS-NCs) can be recognized and bound by the heterodimeric nuclear import receptor karyopherin-α / karyopherin-β 1, and will be translocated through NPCs into the nucleus, where NLS-NCs are released from NPCs with the help of Ran guanosine…”