| pubmed-article:9630243 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9630243 | lifeskim:mentions | umls-concept:C0010834 | lld:lifeskim |
| pubmed-article:9630243 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:9630243 | lifeskim:mentions | umls-concept:C0007610 | lld:lifeskim |
| pubmed-article:9630243 | lifeskim:mentions | umls-concept:C0178735 | lld:lifeskim |
| pubmed-article:9630243 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9630243 | pubmed:dateCreated | 1998-6-30 | lld:pubmed |
| pubmed-article:9630243 | pubmed:abstractText | Nuclear transport is an energy-dependent process mediated by saturable receptors. Import and export receptors are thought to recognize and bind to nuclear localization signals or nuclear export signals, respectively, in the transported molecules. The receptor-substrate interaction can be direct or mediated by an additional adapter protein. The transport receptors dock their cargoes to the nuclear pore complexes (NPC) and facilitate their translocation through the NPC. After delivering their cargoes, the receptors are recycled to initiate additional rounds of transport. Because a transport event for a cargo molecule is unidirectional, the transport receptors engage in asymmetric cycles of translocation across the NPC. The GTPase Ran acts as a molecular switch for receptor-cargo interaction and imparts directionality to the transport process. Recently, the combined use of different in vitro and in vivo approaches has led to the characterization of novel import and export signals and to the identification of the first nuclear import and export receptors. | lld:pubmed |
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