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Targeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane.

dc.contributor.authorBlenski, Marina
dc.contributor.authorKehlenbach, Ralph H.
dc.date.accessioned2019-02-26T14:57:36Z
dc.date.available2019-02-26T14:57:36Z
dc.date.issued2019de
dc.relation.ISSN1422-0067de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/15837
dc.description.abstractLRRC59 (leucine-rich repeat-containing protein 59) is a tail-anchored protein with a single transmembrane domain close to its C-terminal end that localizes to the endoplasmic reticulum (ER) and the nuclear envelope. Here, we investigate the mechanisms of membrane integration of LRRC59 and its targeting to the inner nuclear membrane (INM). Using purified microsomes, we show that LRRC59 can be post-translationally inserted into ER-derived membranes. The TRC-pathway, a major route for post-translational membrane insertion, is not required for LRRC59. Like emerin, another tail-anchored protein, LRRC59 reaches the INM, as demonstrated by rapamycin-dependent dimerization assays. Using different approaches to inhibit importin α/β-dependent nuclear import of soluble proteins, we show that the classic nuclear transport machinery does not play a major role in INM-targeting of LRRC59. Instead, the size of the cytoplasmic domain of LRRC59 is an important feature, suggesting that targeting is governed by passive diffusion.de
dc.description.sponsorshipOpen-Access-Publikationsfonds 2019
dc.languageeng
dc.language.isoengde
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectinner nuclear membrane; tail-anchored proteins; LRRC59; TRC40de
dc.subject.ddc610
dc.titleTargeting of LRRC59 to the Endoplasmic Reticulum and the Inner Nuclear Membrane.de
dc.typejournalArticlede
dc.identifier.doi10.3390/ijms20020334
dc.type.versionpublishedVersionde
dc.bibliographicCitation.volume20de
dc.bibliographicCitation.issue2de
dc.type.subtypejournalArticle
dc.identifier.pmid30650545
dc.bibliographicCitation.articlenumber334de
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalInternational Journal of Molecular Sciencesde


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