Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9021
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dc.contributor.authorEwerling, Alexander-
dc.contributor.authorMaissl, Vanessa-
dc.contributor.authorWickstead, Bill-
dc.contributor.authorMay-Simera, Helen Louise-
dc.date.accessioned2023-04-18T09:48:46Z-
dc.date.available2023-04-18T09:48:46Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9038-
dc.description.abstractThe eukaryotic BBSome is a transport complex within cilia and assembled by chaperonin-like BBS proteins. Recent work indicates nuclear functions for BBS proteins in mammals, but it is unclear how common these are in extant proteins or when they evolved. We screened for BBS orthologues across a diverse set of eukaryotes, consolidated nuclear association via signal sequence predictions and permutation analysis, and validated nuclear localization in mammalian cells via fractionation and immunocytochemistry. BBS proteins are—with exceptions— conserved as a set in ciliated species. Predictions highlight five most likely nuclear proteins and suggest that nuclear roles evolved independently of nuclear access during mitosis. Nuclear localization was confirmed in human cells. These findings suggest that nuclear BBS functions are potentially not restricted tomammals, but may be a common frequently co-opted eukaryotic feature. Understanding the functional spectrum of BBS proteins will help elucidating their role in gene regulation, development, and disease.en_GB
dc.language.isoengde
dc.rightsCC BY-NC-ND*
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleNeofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotesen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9021-
jgu.type.contenttypeScientific articlede
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 10 Biologiede
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleiSciencede
jgu.journal.volume4de
jgu.journal.issue26de
jgu.pages.alternative106410de
jgu.publisher.year2023-
jgu.publisher.nameElsevierde
jgu.publisher.placeAmsterdam ; Bosten ; London ; New York ; Oxford ; Paris ; Philadelphia ; San Diego ; St. Louisde
jgu.publisher.issn2589-0042de
jgu.organisation.placeMainz-
jgu.subject.ddccode570de
jgu.publisher.doi10.1016/ j.isci.2023.106410de
jgu.organisation.rorhttps://ror.org/023b0x485-
jgu.subject.dfgLebenswissenschaftende
Appears in collections:DFG-491381577-G

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