論文

査読有り
2019年4月

Yeast Dop1 is required for glycosyltransferase retrieval from the trans-Golgi network

Biochimica et biophysica acta. General subjects
  • Zhao, Shen-Bao
  • ,
  • Suda, Yasuyuki
  • ,
  • Nakanishi, Hideki
  • ,
  • Wang, Ning
  • ,
  • Yoko-O, Takehiko
  • ,
  • Gao
  • ,
  • Xiao-Dong
  • ,
  • Fujita, Morihisa

1863
6
開始ページ
1147
終了ページ
1157
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bbagen.2019.04.009
出版者・発行元
ELSEVIER SCIENCE BV

[BACKGROUND] Glycosyltransferases are type II membrane proteins that are responsible for glycan modification of proteins and lipids, and localize to distinct cisternae in the Golgi apparatus. During cisternal maturation, retrograde trafficking helps maintain the steady-state localization of these enzymes in the sub-compartments of the Golgi.
[METHODS] To understand how glycosyltransferases are recycled in the late Golgi complex, we searched for genes that are essential for budding yeast cell growth and that encode proteins localized in endosomes and in the Golgi. We specifically analyzed the roles of Dop1 and its binding partner Neo1 in retaining Golgi-resident glycosyltransferases, in the late Golgi complex.
[RESULTS] Dop1 primarily localized to younger compartments of the trans-Golgi network (TGN) and seemed to cycle within the TGN. In contrast, Neo1, a P4-ATPase that interacts with Dop1, localized to the TGN. Abolition of DOP1 expression led to defects in the FM4-64 endocytic pathway. Dop1 and Neo1 were required for correct glycosylation of invertase, a secretory protein, at the Golgi. In DOP1-shutdown cells, Och1, a mannosyltransferase that is typically located in the cis-Golgi

リンク情報
DOI
https://doi.org/10.1016/j.bbagen.2019.04.009