Sucrose starvation induces the degradation of proteins in trans-Golgi network and secretory vesicle cluster in tobacco BY-2 cells. Issue 8 (2nd August 2020)
- Record Type:
- Journal Article
- Title:
- Sucrose starvation induces the degradation of proteins in trans-Golgi network and secretory vesicle cluster in tobacco BY-2 cells. Issue 8 (2nd August 2020)
- Main Title:
- Sucrose starvation induces the degradation of proteins in trans-Golgi network and secretory vesicle cluster in tobacco BY-2 cells
- Authors:
- Oda, Yamato
Asatsuma, Satoru
Nakasone, Hiroaki
Matsuoka, Ken - Abstract:
- ABSTRACT: 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 GRAPHICAL ABSTRACT: uf0001 Modulation of the turnover ofABSTRACT: 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 GRAPHICAL ABSTRACT: uf0001 Modulation of the turnover of endomembrane proteins and of the transport of macromolecules upon sucrose starvation in tobacco BY-2 cells … (more)
- Is Part Of:
- Bioscience, biotechnology, and biochemistry. Volume 84:Issue 8(2020)
- Journal:
- Bioscience, biotechnology, and biochemistry
- Issue:
- Volume 84:Issue 8(2020)
- Issue Display:
- Volume 84, Issue 8 (2020)
- Year:
- 2020
- Volume:
- 84
- Issue:
- 8
- Issue Sort Value:
- 2020-0084-0008-0000
- Page Start:
- 1652
- Page End:
- 1666
- Publication Date:
- 2020-08-02
- Subjects:
- Endomembrane organelle -- pectin -- protein degradation -- secretion -- sugar
Biotechnology -- Periodicals
Biochemistry -- Periodicals
660.6 - Journal URLs:
- https://academic.oup.com/bbb ↗
http://www.tandfonline.com/toc/tbbb20/current ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/09168451.2020.1756736 ↗
- Languages:
- English
- ISSNs:
- 0916-8451
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22687.xml