Evolution and diversification of the nuclear pore complex

Abstract

The nuclear pore complex (NPC) is responsible for transport between the cytoplasm and nucleoplasm and one of the more intricate structures of eukaryotic cells. Typically composed of over 300 polypeptides, the NPC shares evolutionary origins with endo-membrane and intraflagellar transport system complexes. The modern NPC was fully established by the time of the last eukaryotic common ancestor and, hence, prior to eukaryote diversification. Despite the complexity, the NPC structure is surprisingly flexible with considerable variation between lineages. Here, we review diversification of the NPC in major taxa in view of recent advances in genomic and structural characterisation of plant, protist and nucleomorph NPCs and discuss the implications for NPC evolution. Furthermore, we highlight these changes in the context of mRNA export and consider how this process may have influenced NPC diversity. We reveal the NPC as a platform for continual evolution and adaptation.

Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly

“…Multiple copies of the Y-complexes arrange into annular assemblies forming the largest part of the cytoplasmic and nucleoplasmic ring structures of the NPC. Although components of the Y-complexes can be found in all eukaryotes [ 13 , 14 ], the precise arrangement varies between species. In S. cerevisiae , the cytoplasmic and nucleoplasmic rings are each composed of eight Y-complexes, which arrange in a head to tail fashion to form these rings [ 30 , 31 ].…”

“…Although the general structure of NPCs is evolutionarily conserved [ 5 , 12 ], at least in the organisms analyzed, individual nucleoporins often show little conservation between evolutionary distant organisms and only few nucleoporins are found in all species. For example, of the three vertebrate transmembrane nucleoporins, GP210, POM121 and NDC1, only NDC1 and POM121 are more widely conserved, but not found in all species [ 13 , 14 , 15 ]. Thus, additional anchoring points for nucleoporins to the pore membrane must exist.…”

RANBP2 evolution and human disease

“…It is the largest Nup (358 kDa), the main constituent of NPC cytoplasmic fibrils, and appears to have multiple functions, some of which are still debated. While the majority of Nups and the central structures of NPCs are highly conserved across eukaryotes [6,7], some have evolved specifically in metazoans or even vertebrates. RANBP2 is one such example since it is only found in metazoans.…”

Biomedical implications of nuclear transport

“…As a result, perturbations in the homeostasis of NPC or NE biology are implicated in a range of pathological states, such as neurodegenerative or movement disorders, ageing, cancer, acute necrotizing encephalopathy (ANE) and viral infection [2]. Furthermore, variations in the composition and organization of the NPC are now known to occur between evolutionary lineages with likely significant connections with divergent requirements [3]. Here, in the first of two collections devoted to the NPC and associated nuclear components, we have assembled a selection of articles with novel perspectives on biomedical implications of NPC biology and nucleocytoplasmic trafficking.…”