Cell
Volume 82, Issue 3, 11 August 1995, Pages 463-473
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Article
Identification of a signal for rapid export of proteins from the nucleus

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Abstract

Active nuclear import of protein is controlled by nuclear localization signals (NLSs), but nuclear export is not understood well. Nuclear trafficking of the catalytic (C) subunit of CAMP-dependent protein kinase (cAPK) is critical for regulation of gene expression. The heat-stable inhibitor (PKI) of cAPK contains a nuclear export signal (NES) that triggers rapid, active net extrusion of the C-PKI complex from the nucleus. This NES (residues 35–49), fused or conjugated to heterologous proteins, was sufficient for rapid nuclear export. Hydrophobic residues were critical. The NES is a slightly weaker signal than the SV40 NLS. A sequence containing only residues 37–46, LALKLAGLDI, is also sufficient for nuclear export. This is an example of a protein-based NES having no obvious association with RNA. A similar sequence, LQLPPLERLTL, from Rev, an RNA-binding protein of HIV-1, also is an NES.

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