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

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Author(s)

    • 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
    • Goto Satoshi
    • Department of Physiology, Keio University, School of Medicine|Research Group of Glycobiology and Glycotechnology, Mitsubishi-Kagaku Institute of Life Sciences

Abstract

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 <i>Drosophila</i> are GM130, 120 kDa and Syntaxin16 (Syx16); however the anti-120 kDa antibody is no longer available. In the present study, <i>Drosophila</i> 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>

Journal

  • Cell Structure and Function

    Cell Structure and Function 37(1), 55-63, 2012

    Japan Society for Cell Biology

Codes

  • NII Article ID (NAID)
    130004137577
  • Text Lang
    ENG
  • ISSN
    0386-7196
  • Data Source
    J-STAGE 
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