Publications by authors named "J Katahira"

Cell motility is related to the higher-order structure of chromatin. Stimuli that induce cell migration change chromatin organization; such stimuli include elevated histone H3 lysine 9 trimethylation (H3K9me3). We previously showed that depletion of histone H3 lysine 9 methyltransferase, SUV39H1, suppresses directional cell migration.

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To facilitate selfish replication, viruses halt host gene expression in various ways. The nuclear export of mRNA is one such process targeted by many viruses. SARS-CoV-2, the etiological agent of severe acute respiratory syndrome, also prevents mRNA nuclear export.

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Article Synopsis
  • - The LINC complex, made of SUN and nesprin proteins, connects the nucleus to the cytoskeleton and is crucial for processes like cell migration and mechanotransduction from external signals.
  • - SUN1 is essential for directional cell movement, and depletion of SUN1 affects the maturation of focal adhesions by disrupting the incorporation of proteins like vinculin and zyxin, even though it does not affect the initial recruitment of integrin β1.
  • - The study highlights that SUN1's role in the LINC complex is critical for actin organization and traction force generation, suggesting that SUN2 alone cannot compensate for SUN1's function in maintaining cellular adhesion and movement.
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  • The study investigates the oxidation of flavanone compounds (2'-Hydroxyflavanone and its derivatives) by human cytochrome P450 enzymes, focusing on CYP1A1, 1A2, 1B1.1, 1B1.3, and 2A6.
  • Various di-hydroxylated flavanone and flavone products were identified through LC-MS/MS analysis, revealing significant structural insights related to their formation.
  • Results indicate that CYP1 family enzymes demonstrated higher activity in catalyzing these oxidations compared to CYP2A6, with molecular docking studies supporting these findings.
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Article Synopsis
  • The nucleolar structure is influenced by internal factors like metabolism and external factors like mechanical stress, but how these factors shape nucleoli is not fully understood.
  • The study focuses on the role of SUN1 protein splicing variants in determining the shape and number of nucleoli, finding that variants SUN1_888 and SUN1_916 are vital but serve different functions.
  • Depletion of these SUN1 variants not only changes nucleolar morphology but also impacts chromatin structure and histone modification distribution, suggesting that the LINC complex is key in regulating nucleolar characteristics through chromatin interactions.
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