Role of the Drosophila YATA protein in the proper subcellular localization of COPI revealed by in vivo analysis

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  • Saito Maiko
    Department of Biomolecular Science, Faculty of Science, Toho University
  • Nakayama Minoru
    Department of Biomolecular Science, Faculty of Science, Toho University
  • Fujita Kyota
    Department of Neuropathology, Medical Research Institute, Tokyo Medical and Dental University
  • Uchida Atsuko
    Department of Neuroscience, The Ohio State University
  • Yano Hiroyuki
    Technical Section, National Institute of Genetics
  • Goto Satoshi
    Department of Life Science, College of Science, Rikkyo University
  • Okazawa Hitoshi
    Department of Neuropathology, Medical Research Institute, Tokyo Medical and Dental University
  • Sone Masaki
    Department of Biomolecular Science, Faculty of Science, Toho University

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  • Role of the <i>Drosophila</i> YATA protein in the proper subcellular localization of COPI revealed by <i>in vivo</i> analysis

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<p>yata mutants of Drosophila melanogaster exhibit phenotypes including progressive brain shrinkage, developmental abnormalities and shortened lifespan, whereas in mammals, null mutations of the yata ortholog Scyl1 result in motor neuron degeneration. yata mutation also causes defects in the anterograde intracellular trafficking of a subset of proteins including APPL, which is the Drosophila ortholog of mammalian APP, a causative molecule in Alzheimer’s disease. SCYL1 binds and regulates the function of coat protein complex I (COPI) in secretory vesicles. Here, we reveal a role for the Drosophila YATA protein in the proper localization of COPI. Immunohistochemical analyses performed using confocal microscopy and structured illumination microscopy showed that YATA colocalizes with COPI and GM130, a cis-Golgi marker. Analyses using transgenically expressed YATA with a modified N-terminal sequence revealed that the N-terminal portion of YATA is required for the proper subcellular localization of YATA. Analysis using transgenically expressed YATA proteins in which the C-terminal sequence was modified revealed a function for the C-terminal portion of YATA in the subcellular localization of COPI. Notably, when YATA was mislocalized, it also caused the mislocalization of COPI, indicating that YATA plays a role in directing COPI to the proper subcellular site. Moreover, when both YATA and COPI were mislocalized, the staining pattern of GM130 revealed Golgi with abnormal elongated shapes. Thus, our in vivo data indicate that YATA plays a role in the proper subcellular localization of COPI.</p>

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