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Sci Rep. 2014 Apr 11;4:4655. doi: 10.1038/srep04655.

Functional genomics evidence unearths new moonlighting roles of outer ring coat nucleoporins.

Author information

1
Department of Molecular Biology & Genetics, Democritus University of Thrace, GR-68100 Alexandroupolis, Greece.
2
Donnelly Centre for Cellular & Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.
3
Department of Genetics, Development & Molecular Biology, School of Biology, Faculty of Sciences, Aristotle University of Thessaloniki, GR-54124 Thessalonica, Greece.
4
Bioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, PO Box 20537, CY-1678 Nicosia, Cyprus.
5
1] Donnelly Centre for Cellular & Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada [2] Bioinformatics Research Laboratory, Department of Biological Sciences, University of Cyprus, PO Box 20537, CY-1678 Nicosia, Cyprus [3] Institute of Applied Biosciences, Centre for Research & Technology, PO Box 361, GR-57001 Thessalonica, Greece [4].

Abstract

There is growing evidence for the involvement of Y-complex nucleoporins (Y-Nups) in cellular processes beyond the inner core of nuclear pores of eukaryotes. To comprehensively assess the range of possible functions of Y-Nups, we delimit their structural and functional properties by high-specificity sequence profiles and tissue-specific expression patterns. Our analysis establishes the presence of Y-Nups across eukaryotes with novel composite domain architectures, supporting new moonlighting functions in DNA repair, RNA processing, signaling and mitotic control. Y-Nups associated with a select subset of the discovered domains are found to be under tight coordinated regulation across diverse human and mouse cell types and tissues, strongly implying that they function in conjunction with the nuclear pore. Collectively, our results unearth an expanded network of Y-Nup interactions, thus supporting the emerging view of the Y-complex as a dynamic protein assembly with diverse functional roles in the cell.

PMID:
24722254
PMCID:
PMC3983603
DOI:
10.1038/srep04655
[Indexed for MEDLINE]
Free PMC Article

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