Classical nuclear localization signals: Definition, function, and interaction with importin alpha

• Type of Material: Article
• Authors: Allison Lange, Emory University; Ryan E. Mills, Emory University; Christopher J. Lange, Emory University; Murray Stewart, Medical Research Center Laboratory of Molecular Biology; Scott E. Devine, Emory University; Anita Corbett, Emory University
• Language: English
• Date: 2007-02-23
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://dx.doi.org/10.1074/jbc.R600026200
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 282
• Issue: 8
• Start Page: 5101
• End Page: 5105
• Grant/Funding Information: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502416/bin/NIHMS238720-supplement-Supplemental.xls
• Keywords: Life Sciences & Biomedicine; Biochemistry & Molecular Biology; LARGE-T-ANTIGEN; KARYOPHERIN-ALPHA; SACCHAROMYCES-CEREVISIAE; IN-VIVO; SYSTEMS-ANALYSIS; GTPASE-ACTIVATING PROTEIN; CRYSTALLOGRAPHIC ANALYSIS; PORE COMPLEX; STRUCTURAL BASIS; Science & Technology; NUCLEOTIDE EXCHANGE
• Research Categories: Chemistry, Biochemistry

Abstract

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 β, 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.