Planned Member


Principal Investigator
Satoshi Goto
Department of Life Science, College of Science, Rikkyo University

Investigation of sugar chain-modifying sorting zone

Research abstract

Most secretory and plasma membrane proteins are modified with various types of sugar chains (glycans). A number of sugar chain modifications take place in the endoplasmic reticulum and Golgi apparatus. How such various glycosylation reactions are organized in the organelles remains largely unknown. We have proposed subregions conducting different types of glycosylation in the organelles, which is now called “sorting zones” (PNAS 2005). In this project, we are investigating how the sorting zones are formed and what is their biological significances.

Original papers

  1. Yamamoto-Hino,M. and Goto,S. (2016) Spätzle-processing enzyme-independent activation of the Toll pathway in Drosophila innate immunity. Cell Struct. Funct., 41, 55-60
  2. Yamamoto-Hino,M., Muraoka,M., Kondo,S., Ueda,R., Okano,H. and Goto,S. (2015) Dynamic regulation of innate immune responses in Drosophila by Senju-mediated glycosylation. Proc. Natl. Acad. Sci. USA, 112, 5809-5814
  3. Yamamoto-Hino,M., Yoshida,H., Ichimiya,T., Sakamura,S., Maeda,M., Kimura,Y., Sasaki,N., Aoki-Kinoshita,K.Y, Kinoshita-Toyoda,A., Toyoda,H., Ueda,R., Nishihara,S., and Goto,S. (2015) Phenotype-based clustering of glycosylation-related genes by RNAi-mediated gene silencing. Genes Cells, 20, 521-542
  4. Yamamoto-Hino,M., Abe,M., Shibano,T., Setoguchi,Y., Awano,W., Ueda.R., Okano,H. and Goto,S. (2012) Cisterna-specific localization of glycosylation-related proteins to the Golgi apparatus. Cell Struct. Funct., 37, 55-63
  5. Yano,H., Yamamoto-Hino,M., Awano,W., Aoki-Kinoshita,K.F., Tsuda-Sakurai,K., Okano,H. and Goto,S. (2012) Identification of proteasome components required for apical localization of Chaoptin using functional genomics. J. Neurogenet., 26, 53-63
  6. Yamamoto-Hino,M., Kanie,Y., Awano,W., Aoki-Kinoshita,K.F., Yano,H., Nishihara,S., Okano,H., Ueda,R., Kanie,O. and Goto,S. (2010) Identification of genes required for neural-specific glycosylation using functional genomics. PLoS Genetics, 6, e1001254
  7. Mukai,A., Yamamoto-Hino,M., Awano,W., Watanabe,W., Komada,M. and Goto,S. (2010) Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wingless/Wnt. The EMBO J., 29, 2114-2125
  8. Midorikawa,R., Yamamoto-Hino,M., Awano,W., Hinohara,Y., Ueda,R. and Goto,S. (2010) Autophagy-dependent rhodopsin degradation prevents retinal degeneration in DrosophilaJ. Neurosci., 30, 10703-10719
  9. Yano,H., Yamamoto-Hino,M., Abe,M., Kuwahara,R., Haraguchi,S., Kusaka,I., Awano,W., Kinoshita-Toyoda,A., Toyoda,H. and Goto,S. (2005) Distinct functional units of the Golgi complex in Drosophila cells.  Proc. Natl. Acad. Sci. USA 102, 13467-13472
  10. Goto,S., Taniguchi,M., Muraoka,M., Toyoda,H., Sado,Y., Kawakita,M. and Hayashi,S. (2001) UDP-sugar transporter implicated in glycosylation and processing of Notch. Nature Cell Biol., 3, 816-822


  1. Yamamoto-Hino,M. and Goto,S. (2014) Localization of glycosyl enzymes and nucleotide-sugar transporters in the endoplasmic reticulum and the Golgi apparatus. In “Glycoscience: Biology and Medicine” Taniguchi, N. et al. ed. SpringerReference, Heidelberg
  2. Yamamoto-Hino,M., Okano,H., Kanie,O. and Goto,S. (2012) Structure, Function and Formation of Glycans in Drosophila. In “Glycans: Biochemistry, Characterization and Applications.” pp.165-188 Mora Montes, H. M. ed. Nova Science publishers, Inc., NY
  3. Yamamoto-Hino,M. and Goto,S. (2013) In vivo RNAi-based screens: studies in model organisms. Genes, 4, 646-665
  4. Mukai,A., Yamamoto-Hino,M., Komada.M., Okano,H. and Goto,S. (2012) Balanced ubiquitination determines cellular responsiveness to extracellular stimuli. Cellular and Molecular Life Sciences, 69, 4007-4016
  5. Goto,S. (2006) Regulation of glycosylation by Golgi units. Trends in Glycoscience and Glycotechnology 18, 377-382