Cisterna-specific Localization of Glycosylation-related Proteins to the Golgi Apparatus

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  • Yamamoto-Hino Miki
    Department of Physiology, Keio University, School of Medicine Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences
  • Abe Masato
    Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences
  • Shibano Takako
    Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences
  • Setoguchi Yuka
    Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences
  • Awano Wakae
    Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences Mutant Flies Laboratory, Mitsubishi-Kagaku Institute of Life Sciences
  • Ueda Ryu
    Invertebrate Genetics Laboratory, National Institute of Genetics
  • Okano Hideyuki
    Department of Physiology, Keio University, School of Medicine
  • Goto Satoshi
    Department of Physiology, Keio University, School of Medicine Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences

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The Golgi apparatus is an intracellular organelle playing central roles in post-translational modification and in the secretion of membrane and secretory proteins. These proteins are synthesized in the endoplasmic reticulum (ER) and transported to the cis-, medial-and trans-cisternae of the Golgi. While trafficking through the Golgi, proteins are sequentially modified with glycan moieties by different glycosyltransferases. Therefore, it is important to analyze the glycosylation function of the Golgi at the level of cisternae. Markers widely used for cis-, medial- and trans-cisternae/trans Golgi network (TGN) in Drosophila are GM130, 120 kDa and Syntaxin16 (Syx16); however the anti-120 kDa antibody is no longer available. In the present study, Drosophila Golgi complex-localized glycoprotein-1 (dGLG1) was identified as an antigen recognized by the anti-120 kDa antibody. A monoclonal anti-dGLG1 antibody suitable for immunohistochemistry was raised in rat. Using these markers, the localization of glycosyltransferases and nucleotide-sugar transporters (NSTs) was studied at the cisternal level. Results showed that glycosyltransferases and NSTs involved in the same sugar modification are localized to the same cisternae. Furthermore, valuable functional information was obtained on the localization of novel NSTs with as yet incompletely characterized biochemical properties.<br>

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