{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T21:59:00Z","timestamp":1773352740483,"version":"3.50.1"},"reference-count":33,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5930","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2009,5,22]]},"abstract":"<jats:title>Nuclear Import\/Export Receptor<\/jats:title>\n          <jats:p>\n            Nuclear transport receptors constantly shuttle cargo between the nucleus and the cytoplasm through nuclear pore complexes. In the nucleus, RanGTP promotes the dissociation of cargo from importins, which import cargo into the nucleus (where RanGTP is guanosine 5\u2032 triphosphate\u2013bound Ran). Conversely, nuclear RanGTP promotes cargo-binding to exportins, which export cargo from the nucleus. Cargo is released from exportins in the cytoplasm upon hydrolysis of RanGTP. Cytoplasmically assembled RNA splicing components enter the nucleus together with an import adapter snurportin 1 (SPN1), but how then does the import adapter release its cargo and exit the nucleus to collect further cargo? The nuclear exportin CRM1 exports a broad range of substrates\u2014including SPN1, ribosomes, and many regulatory proteins.\n            <jats:bold>\n              Monecke\n              <jats:italic>et al.<\/jats:italic>\n            <\/jats:bold>\n            (p.\n            <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" page=\"1087\" related-article-type=\"in-this-issue\" vol=\"324\" xlink:href=\"10.1126\/science.1173388\">1087<\/jats:related-article>\n            ) describe the crystal structure of CRM1 bound to SPN1 and RanGTP. The structure shows that SPN1 cannot simultaneously bind its import cargo and the exportin CRM1, ensuring that only cargo-free SPN1 is returned to the cytoplasm. There are no direct contacts between Ran and SPN1 in the ternary complex, suggesting that RanGTP promotes cargo-binding through long-range conformational changes in CRM1.\n          <\/jats:p>","DOI":"10.1126\/science.1173388","type":"journal-article","created":{"date-parts":[[2009,4,24]],"date-time":"2009-04-24T01:40:46Z","timestamp":1240537246000},"page":"1087-1091","source":"Crossref","is-referenced-by-count":208,"title":["Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP"],"prefix":"10.1126","volume":"324","author":[{"given":"Thomas","family":"Monecke","sequence":"first","affiliation":[{"name":"Abteilung f\u00fcr Molekulare Strukturbiologie, Institut f\u00fcr Mikrobiologie und Genetik, GZMB, Georg-August-Universit\u00e4t G\u00f6ttingen, Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen, Germany."}]},{"given":"Thomas","family":"G\u00fcttler","sequence":"additional","affiliation":[{"name":"Abteilung Zellul\u00e4re Logistik, Max-Planck-Institut f\u00fcr Biophysikalische Chemie, Am Fassberg 11, 37077 G\u00f6ttingen, Germany."}]},{"given":"Piotr","family":"Neumann","sequence":"additional","affiliation":[{"name":"Abteilung f\u00fcr Molekulare Strukturbiologie, Institut f\u00fcr Mikrobiologie und Genetik, GZMB, Georg-August-Universit\u00e4t G\u00f6ttingen, Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen, Germany."}]},{"given":"Achim","family":"Dickmanns","sequence":"additional","affiliation":[{"name":"Abteilung f\u00fcr Molekulare Strukturbiologie, Institut f\u00fcr Mikrobiologie und Genetik, GZMB, Georg-August-Universit\u00e4t G\u00f6ttingen, Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen, Germany."}]},{"given":"Dirk","family":"G\u00f6rlich","sequence":"additional","affiliation":[{"name":"Abteilung Zellul\u00e4re Logistik, Max-Planck-Institut f\u00fcr Biophysikalische Chemie, Am Fassberg 11, 37077 G\u00f6ttingen, Germany."}]},{"given":"Ralf","family":"Ficner","sequence":"additional","affiliation":[{"name":"Abteilung f\u00fcr 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