Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (23)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Takatsuka, C.
Right arrow Articles by Moriyasu, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Takatsuka, C.
Right arrow Articles by Moriyasu, Y.
Agricola
Right arrow Articles by Takatsuka, C.
Right arrow Articles by Moriyasu, Y.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 2004, Vol. 45, No. 3 265-274
© 2004 Oxford University Press

3-Methyladenine Inhibits Autophagy in Tobacco Culture Cells under Sucrose Starvation Conditions

Chihiro Takatsuka1, Yuko Inoue1, Ken Matsuoka2 and Yuji Moriyasu1,3

1 School of Food and Nutritional Sciences, University of Shizuoka, 52-1 Yada, Shizuoka, 422-8526 Japan
2 RIKEN Plant Science Center, 1-7-22 Suehiro-cho, Yokohama, 230-0045 Japan

Tobacco (Nicotiana tabacum) culture cells perform autophagy and degrade cellular proteins in response to sucrose starvation. When protein degradation is blocked by the cysteine protease inhibitor E-64c, lysosomes containing particles of cytoplasm (autolysosomes) accumulate in the cells. Therefore, using light microscopy, we can determine whether cells have performed autophagy. In this study, we investigated whether or not 3-methyladenine (3-MA), which is a known inhibitor of autophagy in mammalian cells, blocks autophagy in tobacco culture cells. The accumulation of autolysosomes was blocked by the addition to the culture media of 5 mM 3-MA together with E-64c. We did not detect autolysosomes or structures thought to be involved with autophagy, such as autophagosomes, accumulating in these cells, as observed by electron microscopy. 3-MA blocked cellular protein degradation without any effect on cellular protease activity. In mammalian cells, phosphatidylinositol 3-kinase (PtdIns 3-kinase) is a putative target of 3-MA. The PtdIns 3-kinase inhibitors wortmannin and LY294002 also inhibited the accumulation of autolysosomes in tobacco culture cells. These results suggest that (1) 3-MA inhibits autophagy by blocking the formation of autophagosomes in tobacco culture cells, and (2) PtdIns 3-kinase is essential for autophagy in tobacco cells.

3 Corresponding author: E-mail, moriyasu{at}u-shizuoka-ken.ac.jp; Fax, +81-54-264-5099.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
V. Jain, W. Kaiser, and S. C. Huber
Cytokinin Inhibits the Proteasome-Mediated Degradation of Carbonylated Proteins in Arabidopsis Leaves
Plant Cell Physiol., May 1, 2008; 49(5): 843 - 852.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
F. Poustka, N. G. Irani, A. Feller, Y. Lu, L. Pourcel, K. Frame, and E. Grotewold
A Trafficking Pathway for Anthocyanins Overlaps with the Endoplasmic Reticulum-to-Vacuole Protein-Sorting Route in Arabidopsis and Contributes to the Formation of Vacuolar Inclusions
Plant Physiology, December 1, 2007; 145(4): 1323 - 1335.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
Y. Inoue, T. Suzuki, M. Hattori, K. Yoshimoto, Y. Ohsumi, and Y. Moriyasu
AtATG Genes, Homologs of Yeast Autophagy Genes, are Involved in Constitutive Autophagy in Arabidopsis Root Tip Cells
Plant Cell Physiol., December 1, 2006; 47(12): 1641 - 1652.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
Y. Inoue and Y. Moriyasu
Autophagy is not a Main Contributor to the Degradation of Phospholipids in Tobacco Cells Cultured under Sucrose Starvation Conditions
Plant Cell Physiol., April 1, 2006; 47(4): 471 - 480.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
S. Slavikova, G. Shy, Y. Yao, R. Glozman, H. Levanony, S. Pietrokovski, Z. Elazar, and G. Galili
The autophagy-associated Atg8 gene family operates both under favourable growth conditions and under starvation stresses in Arabidopsis plants
J. Exp. Bot., November 1, 2005; 56(421): 2839 - 2849.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. R. Thompson, J. H. Doelling, A. Suttangkakul, and R. D. Vierstra
Autophagic Nutrient Recycling in Arabidopsis Directed by the ATG8 and ATG12 Conjugation Pathways
Plant Physiology, August 1, 2005; 138(4): 2097 - 2110.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
K. Yano, S. Matsui, T. Tsuchiya, M. Maeshima, N. Kutsuna, S. Hasezawa, and Y. Moriyasu
Contribution of the Plasma Membrane and Central Vacuole in the Formation of Autolysosomes in Cultured Tobacco Cells
Plant Cell Physiol., July 15, 2004; 45(7): 951 - 957.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.