Interaction of alpha-taxilin Localized on Intracellular Components with the Microtubule Cytoskeleton

  • Horii Yukimi
    Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University
  • Nogami Satoru
    Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University
  • Kawano Yoji
    Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University
  • Kaneko-Kawano Takako
    Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University
  • Ohtomo Natsuko
    Department of Gastroenterology, Graduate School of Medicine, The University of Tokyo
  • Tomiya Tomoaki
    Department of Gastroenterology, Graduate School of Medicine, The University of Tokyo
  • Shirataki Hiromichi
    Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University

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  • Interaction of α-taxilin Localized on Intracellular Components with the Microtubule Cytoskeleton

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Intracellular vesicle traffic plays an essential role in the establishment and maintenance of organelle identity and biosynthetic transport. We have identified α-taxilin as a binding partner of the syntaxin family, which is involved in intracellular vesicle traffic. Recently, we have found that α-taxilin is over-expressed in malignant tissues including hepatocellular carcinoma and renal cell carcinoma. However, a precise role of α-taxilin in intracellular vesicle traffic and carcinogenesis remains unclear. Then, we first investigated here the intracellular distribution of α-taxilin in Hela cells. Immunofluorescence studies showed that α-taxilin distributes throughout the cytoplasm and exhibits a tubulo-vesicular pattern. Biochemical studies showed that α-taxilin is abundantly localized on intracellular components as a peripheral membrane protein. Moreover, we found that α-taxilin distributes in microtubule-dependent and syntaxin-independent manners, that α-taxilin directly binds to polymerized tubulin in vitro, and that N-ethylmaleimide but not brefeldin A affects the intracellular distribution of α-taxilin. These results indicate that α-taxilin is localized on intracellular components in a syntaxin-independent manner and that the α-taxilin-containing intracellular components are associated with the microtubule cytoskeleton and suggest that α-taxilin functions as a linker protein between the α-taxilin-containing intracellular components and the microtubule cytoskeleton.

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