Dual roles of the N-terminal coiled-coil domain of an Aplysia sec7 protein: homodimer formation and nuclear export

Cited 5 time in webofscience Cited 0 time in scopus
  • Hit : 528
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorJun, Yong-Wooko
dc.contributor.authorLee, Seung-Heeko
dc.contributor.authorShim, Jaehoonko
dc.contributor.authorLee, Jin-Ako
dc.contributor.authorLim, Chae-Seokko
dc.contributor.authorKaang, Bong-Kiunko
dc.contributor.authorJang, Deok-Jinko
dc.date.accessioned2017-01-23T02:50:32Z-
dc.date.available2017-01-23T02:50:32Z-
dc.date.created2017-01-04-
dc.date.created2017-01-04-
dc.date.created2017-01-04-
dc.date.created2017-01-04-
dc.date.issued2016-12-
dc.identifier.citationJOURNAL OF NEUROCHEMISTRY, v.139, no.6, pp.1102 - 1112-
dc.identifier.issn0022-3042-
dc.identifier.urihttp://hdl.handle.net/10203/220146-
dc.description.abstractCytohesin family proteins act as guanine nucleotide exchange factors (GEFs) for the ADP-ribosylation factor family of small GTP-binding proteins. Aplysia Sec7 (ApSec7), a member of the cytohesin family in Aplysia, plays key roles in neurite outgrowth in Aplysia neurons. Although ApSec7 has a conserved coiled-coil (CC) domain, its role was not clear. In this study, we found that the CC domain of ApSec7 and ARNO/cytohesin 2 are involved in homodimer formation, leading to efficient plasma membrane targeting of ApSec7 and ARNO/cytohesin 2 in HEK293T cells. Therefore, deletion of the CC domain of ApSec7 and ARNO/cytohesin 2 may result in a loss of dimerization and reduce plasma membrane localization. In addition, the CC domains of ApSec7 and ARNO/cytohesin 2 have partially or fully CRM1-dependent nuclear export signals, respectively. Taken together, our results suggest that the CC domain of cytohesin family proteins, including ApSec7 and ARNO/cytohesin 2, has dual roles in intracellular targeting: increased plasma membrane targeting through homodimer formation and nuclear exclusion through either a CRM1-dependent or a CRM1-independent pathway.-
dc.languageEnglish-
dc.publisherWILEY-BLACKWELL-
dc.subjectNUCLEOTIDE EXCHANGE FACTORS-
dc.subjectCYTOHESIN/ARNO FAMILY-
dc.subjectFACTORS INTERACTS-
dc.subjectLOCALIZATION-
dc.subjectSIGNALS-
dc.subjectBINDING-
dc.subjectASSOCIATION-
dc.subjectEXPRESSION-
dc.subjectSEQUENCE-
dc.subjectDATABASE-
dc.titleDual roles of the N-terminal coiled-coil domain of an Aplysia sec7 protein: homodimer formation and nuclear export-
dc.typeArticle-
dc.identifier.wosid000393038700012-
dc.identifier.scopusid2-s2.0-85006483389-
dc.type.rimsART-
dc.citation.volume139-
dc.citation.issue6-
dc.citation.beginningpage1102-
dc.citation.endingpage1112-
dc.citation.publicationnameJOURNAL OF NEUROCHEMISTRY-
dc.identifier.doi10.1111/jnc.13875-
dc.contributor.localauthorLee, Seung-Hee-
dc.contributor.nonIdAuthorJun, Yong-Woo-
dc.contributor.nonIdAuthorShim, Jaehoon-
dc.contributor.nonIdAuthorLee, Jin-A-
dc.contributor.nonIdAuthorLim, Chae-Seok-
dc.contributor.nonIdAuthorKaang, Bong-Kiun-
dc.contributor.nonIdAuthorJang, Deok-Jin-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorARNO/cytohesin 2-
dc.subject.keywordAuthorcoiled-coil domain-
dc.subject.keywordAuthorcytohesin family-
dc.subject.keywordAuthordimerization-
dc.subject.keywordAuthornuclear export signal-
dc.subject.keywordAuthorSec7 protein-
dc.subject.keywordPlusNUCLEOTIDE EXCHANGE FACTORS-
dc.subject.keywordPlusCYTOHESIN/ARNO FAMILY-
dc.subject.keywordPlusFACTORS INTERACTS-
dc.subject.keywordPlusLOCALIZATION-
dc.subject.keywordPlusSIGNALS-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusASSOCIATION-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusSEQUENCE-
dc.subject.keywordPlusDATABASE-
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 5 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0