REVIEW: Nucleocytoplasmic Transport of Proteins

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A. V. Sorokin, E. R. Kim, and L. P. Ovchinnikov^*

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: p50@rambler.ru; ovchinn@vega.protres.ru

^* To whom correspondence should be addressed.

Received April 10, 2007

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In eukaryotic cells, the movement of macromolecules between the nucleus and cytoplasm occurs through the nuclear pore complex (NPC)--a large protein complex spanning the nuclear envelope. The nuclear transport of proteins is usually mediated by a family of transport receptors known as karyopherins. Karyopherins bind to their cargoes via recognition of nuclear localization signal (NLS) for nuclear import or nuclear export signal (NES) for export to form a transport complex. Its transport through NPC is facilitated by transient interactions between the karyopherins and NPC components. The interactions of karyopherins with their cargoes are regulated by GTPase Ran. In the current review, we describe the NPC structure, NLS, and NES, as well as the model of classic Ran-dependent transport, with special emphasis on existing alternative mechanisms; we also propose a classification of the basic mechanisms of protein transport regulation.

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KEY WORDS: nucleocytoplasmic transport, nuclear pore complex, nucleoporin, exportin, importin, karyopherin, nuclear export signal, nuclear localization signal, Ran

DOI: 10.1134/S0006297907130032

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