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功能基因组学证据揭示了外环核孔蛋白新的兼职功能。

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

作者信息

Katsani Katerina R, Irimia Manuel, Karapiperis Christos, Scouras Zacharias G, Blencowe Benjamin J, Promponas Vasilis J, Ouzounis Christos A

机构信息

Department of Molecular Biology & Genetics, Democritus University of Thrace, GR-68100 Alexandroupolis, Greece.

Donnelly Centre for Cellular & Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada.

出版信息

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

DOI:10.1038/srep04655
PMID:24722254
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3983603/
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.

摘要

越来越多的证据表明,Y复合体核孔蛋白(Y-Nups)参与了真核生物核孔内核之外的细胞过程。为了全面评估Y-Nups可能的功能范围,我们通过高特异性序列图谱和组织特异性表达模式来界定它们的结构和功能特性。我们的分析证实,Y-Nups存在于整个真核生物中,具有新颖的复合结构域架构,支持其在DNA修复、RNA加工、信号传导和有丝分裂控制中的新兼职功能。与发现的部分结构域相关的Y-Nups在不同的人类和小鼠细胞类型及组织中受到严格的协同调控,这强烈暗示它们与核孔协同发挥作用。总体而言,我们的结果揭示了一个扩展的Y-Nup相互作用网络,从而支持了Y复合体作为一种在细胞中具有多种功能作用的动态蛋白质组装体这一新兴观点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/665530a649e5/srep04655-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/2502c3933695/srep04655-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/acd633efd84b/srep04655-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/b8f8e1d7d73d/srep04655-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/0aea5330ab3b/srep04655-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/665530a649e5/srep04655-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/2502c3933695/srep04655-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/acd633efd84b/srep04655-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/b8f8e1d7d73d/srep04655-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/0aea5330ab3b/srep04655-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ebfc/3983603/665530a649e5/srep04655-f5.jpg

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