Please use this identifier to cite or link to this item:
http://doi.org/10.25358/openscience-9021
Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Ewerling, Alexander | - |
dc.contributor.author | Maissl, Vanessa | - |
dc.contributor.author | Wickstead, Bill | - |
dc.contributor.author | May-Simera, Helen Louise | - |
dc.date.accessioned | 2023-04-18T09:48:46Z | - |
dc.date.available | 2023-04-18T09:48:46Z | - |
dc.date.issued | 2023 | - |
dc.identifier.uri | https://openscience.ub.uni-mainz.de/handle/20.500.12030/9038 | - |
dc.description.abstract | The 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.iso | eng | de |
dc.rights | CC BY-NC-ND | * |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject.ddc | 570 Biowissenschaften | de_DE |
dc.subject.ddc | 570 Life sciences | en_GB |
dc.title | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes | en_GB |
dc.type | Zeitschriftenaufsatz | de |
dc.identifier.doi | http://doi.org/10.25358/openscience-9021 | - |
jgu.type.contenttype | Scientific article | de |
jgu.type.dinitype | article | en_GB |
jgu.type.version | Published version | de |
jgu.type.resource | Text | de |
jgu.organisation.department | FB 10 Biologie | de |
jgu.organisation.number | 7970 | - |
jgu.organisation.name | Johannes Gutenberg-Universität Mainz | - |
jgu.rights.accessrights | openAccess | - |
jgu.journal.title | iScience | de |
jgu.journal.volume | 4 | de |
jgu.journal.issue | 26 | de |
jgu.pages.alternative | 106410 | de |
jgu.publisher.year | 2023 | - |
jgu.publisher.name | Elsevier | de |
jgu.publisher.place | Amsterdam ; Bosten ; London ; New York ; Oxford ; Paris ; Philadelphia ; San Diego ; St. Louis | de |
jgu.publisher.issn | 2589-0042 | de |
jgu.organisation.place | Mainz | - |
jgu.subject.ddccode | 570 | de |
jgu.publisher.doi | 10.1016/ j.isci.2023.106410 | de |
jgu.organisation.ror | https://ror.org/023b0x485 | - |
jgu.subject.dfg | Lebenswissenschaften | de |
Appears in collections: | DFG-491381577-G |
Files in This Item:
File | Description | Size | Format | ||
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neofunctionalization_of_cilia-20230418114358788.pdf | 7.64 MB | Adobe PDF | View/Open |