An Intracellular Fragment of Osteoactivin Formed by Ectodomain Shedding Translocated to the Nucleoplasm and Bound to RNA Binding Proteins

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Author(s)

    • OWAKI Kanako OWAKI Kanako
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • YANO Momoko
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • OTO Takahiro
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • SUZUKI Eri
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • TAMURA Seiko
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • ABE Tomoki
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • KOHNO Shohei
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • OHNO Ayako
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • HIRASAKA Katsuya
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • TESHIMA KONDOH Shigetada
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School
    • NIKAWA Takeshi
    • Department of Nutritional Physiology, Institute of Health Biosciences, The University of Tokushima Graduate School

Abstract

Osteoactivin is a type I transmembrane protein upregulated by unloading stresses, including denervation, prolonged bed rest, and space flight, but the regulatory mechanisms of its expression and activation under these conditions remain undefined. Here we report that osteoactivin protein exists in two forms: an intact transmembrane form and a secreted form. The secreted form, the extracellular fragment of osteoactivin, was produced by ectodomain shedding and was released into a culture medium. Amino acid sequence analysis of the carboxy-terminal fragment of osteoactivin (OA-CTF) revealed that cleavage of osteoactivin by proteases occurred both at the cell surface and within the cell membrane. Localization analysis demonstrated translocalization of OA-CTF to the nucleus and the endoplasmic reticulum. Moreover, RNA binding proteins, which regulate pre-mRNA splicing, were identified as OA-CTF binding proteins. These results suggest that OA-CTF formed by ectodomain shedding is involved in the regulation of pre-mRNA splicing.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 76(12), 2225-2229, 2012-12-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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Codes

  • NII Article ID (NAID)
    10031146836
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    09168451
  • NDL Article ID
    024165218
  • NDL Call No.
    Z53-G223
  • Data Source
    CJP  NDL  J-STAGE 
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