Nuclear translocation of RanGAP1 coincides with virtual nuclear envelope breakdown in fission yeast meiosis

Asakawa, Haruhiko; Hiraoka, Yasushi; Haraguchi, Tokuko

doi:10.4161/cib.4.3.14808

Cited by 7 publications

(4 citation statements)

References 24 publications

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“…In these organisms, ELYS appears critical for recruiting the Nup107/160 complex as well as other Nups, essentially merging the two mechanisms as described for mammalian cells (59). Additional cryptic remodeling of the NPC has been observed in Schizosaccharomyces pombe, where during meiosis exclusion of RanGAP from the nucleus is lost, resulting in complete breakdown of nucleocytoplasmic transport, and which may hint at rather more extensive NPC remodeling processes accompanying mitosis than so far uncovered (67). Overall, what these examples are probably indicating is that the underlying mechanisms for control of the NPC are intimately entwined with the mitotic apparatus, even in cells where the NE does not break down, and that at their core these are probably also a highly conserved pathways.…”

Section: Assembly Mitosis and The Npcmentioning

confidence: 85%

Enriching the Pore: Splendid Complexity from Humble Origins

Field

Kořený

Rout

2014

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The nucleus is the defining intracellular organelle of eukaryotic cells and represents a major structural innovation that differentiates the eukaryotic and prokaryotic cellular form. The presence of a nuclear envelope (NE) encapsulating the nucleus necessitates a mechanism for interchange between the contents of the nuclear interior and the cytoplasm, which is mediated via the nuclear pore complex (NPC), a large protein assembly residing in nuclear pores in the NE. Recent advances have begun to map the structure and functions of the NPC in multiple organisms, and to allow reconstruction of some of the evolutionary events that underpin the modern NPC form, highlighting common and differential NPC features across the eukaryotes. Here we discuss some of these advances and the questions being pursued, consider how the evolution of the NPC has been constrained, and finally propose a model for how the nuclear pore complex evolved.

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Section: Assembly Mitosis and The Npcmentioning

confidence: 85%

Enriching the Pore: Splendid Complexity from Humble Origins

Field

Kořený

Rout

2014

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“…Surprisingly, the preference of smaller proteins and smaller extraluminal domains was lost in gametes compared to mitotic cells, indicating that gametes undergo a change in the nuclear permeability barrier. In fission yeast, the NE diffusion barrier is compromised during early anaphase B of meiosis II in a phenomenon known as virtual NE breakdown (vNEBD) ( Arai et al 2010 ; Asakawa et al 2011 ). During vNEBD, NPCs remain intact, but a change in localization of the RanGAP1 from the cytoplasm to the nucleus leads to a collapse of the Ran-GTP gradient.…”

Section: Discussionmentioning

confidence: 99%

A distinct inner nuclear membrane proteome inSaccharomyces cerevisiaegametes

Shelton

Smith

Unruh

et al. 2021

G3 Genes|Genomes|Genetics

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The inner nuclear membrane (INM) proteome regulates gene expression, chromatin organization, and nuclear transport; however, it is poorly understood how changes in INM protein composition contribute to developmentally regulated processes, such as gametogenesis. We conducted a screen to determine how the INM proteome differs between mitotic cells and gametes. In addition, we used a strategy that allowed us to determine if spores synthesize their INM proteins de novo, rather than inheriting their INM proteins from the parental cell. This screen used a split-GFP complementation system, where we were able to compare the distribution of all C-terminally tagged transmembrane proteins in Saccharomyces cerevisiae in gametes to that of mitotic cells. Gametes contain a distinct INM proteome needed to complete gamete formation, including expression of genes linked to cell wall biosynthesis, lipid biosynthetic and metabolic pathways, protein degradation, and unknown functions. Based on the inheritance pattern, INM components are made de novo in the gametes. Whereas mitotic cells show a strong preference for proteins with small extraluminal domains, gametes do not exhibit this size preference likely due to the changes in the nuclear permeability barrier during gametogenesis. Taken together, our data provide evidence for INM changes during gametogenesis and shed light on mechanisms used to shape the INM proteome of spores.

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“…During mitosis in higher eukaryotic cells, NEBD leads to the disassembly of the nuclear membrane and NPC. 26 The spatial connection between the nucleus and cytoplasm, genome organization and stability, and gene expression are all intimately related to NPC proteins. 27,28 Between NEBD and pre-anaphase, when chromosomes align on the metaphase plate, it is essentially free of membranes to allow separation.…”

Section: Discussionmentioning

confidence: 99%

Zap70 and downstreamRanBP2are required for the exact timing of the meiotic cell cycle in oocytes

Kim

Lee

et al. 2017

Cell Cycle

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In previous studies, we observed that Zeta-chain-associated protein kinase 70 (Zap70) regulates spindle assembly and chromosome alignment in mouse oocyte and that Ran binding protein 2 (RanBP2) is a highly associated gene with Zap70 based on a microarray analysis. Because RanBP2 is related to nuclear envelope breakdown (NEBD) during mitosis, the aim of the present study was to elucidate the molecular mechanism of Zap70 with respect to RanBP2 in the germinal vesicle breakdown (GVBD) of oocytes. Results indicated that RanBP2 expression was regulated by Zap70 and that depletion of RanBP2 using RanBP2 RNAi manifested comparable phenotypes to those observed in Zap70 RNAi-treated oocytes, which presented faster processing of GVBD. Additionally, Zap70 RNAi-treated oocytes showed faster meiotic resumption with premature activation of maturation-promoting factor (MPF), premature division of chromosomes at approximately 6-8 h and more rapid degradation of securin. In conclusion, we report that Zap70 is a crucial factor for controlling the exact timing of meiotic progression in mouse oocytes.

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Nuclear translocation of RanGAP1 coincides with virtual nuclear envelope breakdown in fission yeast meiosis

Cited by 7 publications

References 24 publications

Enriching the Pore: Splendid Complexity from Humble Origins

Enriching the Pore: Splendid Complexity from Humble Origins

A distinct inner nuclear membrane proteome inSaccharomyces cerevisiaegametes

Zap70 and downstreamRanBP2are required for the exact timing of the meiotic cell cycle in oocytes

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