Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes
Summary: 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 acros...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-04-01
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| Series: | iScience |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S258900422300487X |
| _version_ | 1797856412786753536 |
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| author | Alexander Ewerling Vanessa Maissl Bill Wickstead Helen Louise May-Simera |
| author_facet | Alexander Ewerling Vanessa Maissl Bill Wickstead Helen Louise May-Simera |
| author_sort | Alexander Ewerling |
| collection | DOAJ |
| description | Summary: 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 to mammals, 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. |
| first_indexed | 2024-04-09T20:40:03Z |
| format | Article |
| id | doaj.art-5b3a20f0342740d3975a4b68a4ccc704 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-04-09T20:40:03Z |
| publishDate | 2023-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-5b3a20f0342740d3975a4b68a4ccc7042023-03-30T04:26:55ZengElsevieriScience2589-00422023-04-01264106410Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotesAlexander Ewerling0Vanessa Maissl1Bill Wickstead2Helen Louise May-Simera3Institute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, GermanyInstitute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, GermanySchool of Life Sciences, University of Nottingham, Nottingham, UKInstitute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, Germany; Corresponding authorSummary: 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 to mammals, 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.http://www.sciencedirect.com/science/article/pii/S258900422300487XMolecular biologyEvolutionary biologyCell biology |
| spellingShingle | Alexander Ewerling Vanessa Maissl Bill Wickstead Helen Louise May-Simera Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes iScience Molecular biology Evolutionary biology Cell biology |
| title | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| title_full | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| title_fullStr | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| title_full_unstemmed | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| title_short | Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| title_sort | neofunctionalization of ciliary bbs proteins to nuclear roles is likely a frequent innovation across eukaryotes |
| topic | Molecular biology Evolutionary biology Cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S258900422300487X |
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