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Critical Reviews™ in Eukaryotic Gene Expression
IF: 1.841 5-Year IF: 1.927 SJR: 0.649 SNIP: 0.516 CiteScore™: 1.96

ISSN Print: 1045-4403
ISSN Online: 2162-6502

Critical Reviews™ in Eukaryotic Gene Expression

DOI: 10.1615/CritRevEukarGeneExpr.v7.i1-2.40
pages 61-72

Molecular Mechanisms of Nuclear Protein Transport

Junona Moroianu
Laboratory of Cell Biology, Rockefeller University, New York, NY 10021


Transport of proteins into and out of the nucleus occurs through nuclear pore complexes (NPC). A heterodimeric protein complex, composed of karyopherin a and β (or importin α and β) functions to target proteins containing a nuclear localization sequence (NLS) to the NPCs. Two additional proteins, the GTPase Ran and p10, are required to translocate the docked NLS protein into the nucleus. The α subunit of karyopherin functions as the NLS receptor, whereas the β subunit mediates docking to nucleoporins that contain peptide repeats. During import the karyopherin heterodimer dissociates: karyopherin α and import substrates enter and accumulate in the nucleoplasm, whereas karyopherin β accumulates at the nuclear pore complex. Ran-GTP induces dissociation of karyopherin α from β by forming a complex with karyopherin β and promotes the release of both karyopherin subunits from a docking site. Protein transport across the NPC may occur via guided diffusion involving the karyopherin-mediated docking and undocking of import substrate to multiple binding sites that extend from the cytoplasmic to the nucleoplasmic ends of the NPC.

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