Sucrose starvation induces the degradation of proteins in trans-Golgi network and secretory vesicle cluster in tobacco BY-2 cells

Yamato Oda, Satoru Asatsuma, Hiroaki Nakasone, Ken Matsuoka

研究成果: Contribution to journalArticle

抜粋

Endomembrane transport system begins at the endoplasmic reticulum (ER), continues to the Golgi apparatus and subsequent compartment called trans-Golgi network (TGN). We found that SUT2, a tobacco sucrose-transporter ortholog and was localized in the TGN, decreased significantly under a sucrose-starvation condition. The tobacco SNARE protein SYP41, localized in the TGN and secretory vesicle cluster (SVC), also decreased under the starvation. Similarly, the SCAMP2-RFP fusion protein, which is localized in TGN, SVC, and plasma membrane (PM), was distributed solely in the PM under the starvation. Under the same starvation condition, protein secretion was not arrested but pectin deposition to cell wall was suppressed. These data indicated that the protein composition in TGN and existence of the SVC are regulated by sugar availability. Furthermore, our findings as well as the involvement of SVC in pectin secretion suggested that synthesis and transport of pectin are regulated by the level of extracellular sugars. Abbreviations: ER: endoplasmic reticulum; GI-TGN: Golgi-released independent TGN; GFP: green fluorescent protein; mRFP: monomeric red fluorescent protein; P4H1.1: prolyl 4-hydroxylase 1.1; PM: plasma membrane; SCAMP2: secretory carrier membrane protein 2; SUT2: sucrose transporter 2; SVC: secretory vesicle cluster; SYP41: syntaxin of plant 41; TGN: trans-Golgi network; YFP: yellow fluorescent protein.

元の言語英語
ページ(範囲)1652-1666
ページ数15
ジャーナルBioscience, Biotechnology and Biochemistry
84
発行部数8
DOI
出版物ステータス出版済み - 8 2 2020

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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