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J. Biol. Chem., Vol. 282, Issue 8, 5101-5105, February 23, 2007
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Minireview
Classical Nuclear Localization Signals: Definition, Function, and Interaction with Importin 
*
1
From the
Department of Biochemistry, School of Medicine, Emory University, Atlanta, Georgia 30322 and Medical Research Center Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom
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 
-karyopherin importin , which mediates interactions with the nuclear pore complex, and the adaptor protein importin 
, 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.
* This minireview will be reprinted in the 2007 Minireview Compendium, which will be available in January, 2008. This work is dedicated to the memory of our friend and colleague, Dr. Alec E. Hodel.
The on-line version of this article (available at http://www.jbc.org) contains a supplemental table.
1 To whom correspondence should be addressed. Tel.: 404-727-4546; Fax: 404-727-2738; E-mail: acorbe2{at}emory.edu.
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