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© The Rockefeller University Press, 0021-9525/1999//435 $5.00
The Journal of Cell Biology, Volume 147, Number 2, , 1999 435-446

Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast

^a Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan
^b Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, Mejirodai, Bunkyo-ku, Tokyo 112-8681, Japan
^c Department of Biosciences, Teikyo University of Science and Technology, Yamanashi 409-0193, Japan
Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan.81-564-55-751681-564-55-7515

yohsumi{at}nibb.ac.jp

We characterized Apg8/Aut7p essential for autophagy in yeast. Apg8p was transcriptionally upregulated in response to starvation and mostly existed as a protein bound to membrane under both growing and starvation conditions. Immunofluorescence microscopy revealed that the intracellular localization of Apg8p changed drastically after shift to starvation. Apg8p resided on unidentified tiny dot structures dispersed in the cytoplasm at growing phase. During starvation, it was localized on large punctate structures, some of which were confirmed to be autophagosomes and autophagic bodies by immuno-EM. Besides these structures, we found that Apg8p was enriched on isolation membranes and in electron less-dense regions, which should contain Apg8p-localized membrane- or lipid-containing structures. These structures would represent intermediate structures during autophagosome formation. Here, we also showed that microtubule does not play an essential role in the autophagy in yeast. The result does not match with the previously proposed role of Apg8/Aut7p, delivery of autophagosome to the vacuole along microtubule. Moreover, it is revealed that autophagosome formation is severely impaired in the apg8 null mutant. Apg8p would play an important role in the autophagosome formation.

Key Words: autophagy • autophagosome • Apg8/Aut7p • Saccharomyces cerevisiae • vacuole

© 1999 The Rockefeller University Press

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• Noda, T., Kim, J., Huang, W.-P., Baba, M., Tokunaga, C., Ohsumi, Y., Klionsky, D. J. (2000). Apg9p/Cvt7p Is an Integral Membrane Protein Required for Transport Vesicle Formation in the Cvt and Autophagy Pathways. JCB 148: 465-480 [Abstract] [Full Text]  
• Paz, Y., Elazar, Z., Fass, D. (2000). Structure of GATE-16, Membrane Transport Modulator and Mammalian Ortholog of Autophagocytosis Factor Aut7p. J. Biol. Chem. 275: 25445-25450 [Abstract] [Full Text]  
• Tanida, I., Tanida-Miyake, E., Ueno, T., Kominami, E. (2001). The Human Homolog of Saccharomyces cerevisiae Apg7p Is a Protein-activating Enzyme for Multiple Substrates Including Human Apg12p, GATE-16, GABARAP, and MAP-LC3. J. Biol. Chem. 276: 1701-1706 [Abstract] [Full Text]  
• Legesse-Miller, A., Sagiv, Y., Glozman, R., Elazar, Z. (2000). Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes. J. Biol. Chem. 275: 32966-32973 [Abstract] [Full Text]  
• Komatsu, M., Tanida, I., Ueno, T., Ohsumi, M., Ohsumi, Y., Kominami, E. (2001). The C-terminal Region of an Apg7p/Cvt2p Is Required for Homodimerization and Is Essential for Its E1 Activity and E1-E2 Complex Formation. J. Biol. Chem. 276: 9846-9854 [Abstract] [Full Text]  
• Chan, T.-F., Bertram, P. G., Ai, W., Zheng, X. F. S. (2001). Regulation of APG14 Expression by the GATA-type Transcription Factor Gln3p. J. Biol. Chem. 276: 6463-6467 [Abstract] [Full Text]  
• Wang, C.-W., Kim, J., Huang, W.-P., Abeliovich, H., Stromhaug, P. E., Dunn, W. A. Jr., Klionsky, D. J. (2001). Apg2 Is a Novel Protein Required for the Cytoplasm to Vacuole Targeting, Autophagy, and Pexophagy Pathways. J. Biol. Chem. 276: 30442-30451 [Abstract] [Full Text]  

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