Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes.
| Autor: | Ewerling A; Institute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, Germany., Maissl V; Institute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, Germany., Wickstead B; School of Life Sciences, University of Nottingham, Nottingham, UK., May-Simera HL; Institute of Molecular Physiology, Faculty of Biology, Johannes Gutenberg-University Mainz, Mainz, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | IScience [iScience] 2023 Mar 16; Vol. 26 (4), pp. 106410. Date of Electronic Publication: 2023 Mar 16 (Print Publication: 2023). |
| DOI: | 10.1016/j.isci.2023.106410 |
| Abstrakt: | 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. Competing Interests: The authors declare no competing interests. (© 2023 The Authors.) |
| Databáze: | MEDLINE |
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