Edited by Haruki NakamuraMitochondria play an important role in energy conversion as well as in intracellular calcium (Ca 2+ ) storage. Ca 2+ uptake from the cytosol to the mitochondria is mediated by the calcium uniporter, which functions as a Ca 2+ ion channel. However, the molecular composition of this uniporter has remained unclear until recently. The Ca 2+ ion channel consists of seven subunits. The yeast reconstitution technique revealed that the mitochondrial calcium uniporter (MCU) and essential MCU regulatory element (EMRE) are the core subunits of the complex. Furthermore, detailed structure-function analyses of the core subunits (MCU and EMRE) were performed. In this review, the regulatory mechanism of mitochondrial Ca 2+ uptake is discussed.
Interleukin-1α (IL-1α), a cytokine released by necrotic cells, causes sterile inflammation. On the other hand, IL-1α is present in the nucleus and also regulates the expression of many proteins. A protein substrate containing a nuclear localization signal (NLS) typically forms a substrate/importin α/β complex, which is subsequently transported to the nucleus. To the best of our knowledge, no study has directly investigated whether IL-1α—which includes NLS—is imported into the nucleus in an importin-dependent manner. In this study, we noted that all detected importin subtypes interacted with IL-1α. In HeLa cells, importin α1-mediated nuclear translocation of IL-1α occurred at steady state and was independent of importin β1. Importin α1 not only was engaged in IL-1α nuclear transport but also concurrently functioned as a molecule that regulated IL-1α protein level in the cell. Furthermore, we discussed the underlying mechanism of IL-1α nuclear translocation by importin α1 based on our findings.
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