Eukaryotic cells have passage holes called "nuclear pore complexes" for transporting molecules between the nucleus and cytoplasm.The "outer rings", which are symmetrically arranged inside the nuclear pores and on the cytoplasmic side, are the foundations that support the nuclear pore complex, and are very similar to humans and budding yeasts, which are evolutionarily distant organisms. Therefore, it has been thought that all living things have the same structure.

 However, this time, a research group at Osaka University has revealed for the first time in the world that the outer ring structure of the nuclear pore complex of fission yeast is completely different from the structure of other previously known creatures.

 The research group analyzed the localization of approximately 30 proteins that make up the nuclear pore complex of fission yeast using immunoelectron microscopy and high-precision fluorescence microscopy.As a result, in humans and Saccharomyces cerevisiae, the same amount of outer ring protein is present on both the inside of the nucleus and the cytoplasmic side, whereas in fission yeast, some proteins are inside the nucleus and others are on the cytoplasmic side. It was found that it was separated and localized.That is, while the outer ring of human and Saccharomyces cerevisiae has a vertically symmetrical structure, the outer ring of fission yeast is divided into two parts and arranged in the nuclear pore complex on the inside of the nucleus and on the cytoplasmic side. It turned out that it was.

 From this result, it has become clear that the structure of the outer ring of the nuclear pore complex is not always common to all eukaryotes, and that it may have various structures depending on the species.In recent years, it has been reported that mutations in the outer ring structure cause nephrotic syndrome, which is a renal disease.This result is expected to advance research on the structure and role of the nuclear pore complex and contribute to the understanding of diseases caused by abnormalities in the nuclear pores.

Paper information:[PLOS Genetics] Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast

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