Characterization of a novel autophagy-specific gene, ATG29
- Department of Biology, Graduate School of Science and Technology, Kobe University, Kobe 657-8501 (Japan)
- Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585 (Japan)
- Department of Bioscience, Teikyo University of Science and Technology, Yamanashi 409-0193 (Japan)
- Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585 (Japan) and School of Life Science, Graduate University for Advance Studies, Okazaki 444-8585 (Japan)
Autophagy is a process whereby cytoplasmic proteins and organelles are sequestered for bulk degradation in the vacuole/lysosome. At present, 16 ATG genes have been found that are essential for autophagosome formation in the yeast Saccharomyces cerevisiae. Most of these genes are also involved in the cytoplasm to vacuole transport pathway, which shares machinery with autophagy. Most Atg proteins are colocalized at the pre-autophagosomal structure (PAS), from which the autophagosome is thought to originate, but the precise mechanism of autophagy remains poorly understood. During a genetic screen aimed to obtain novel gene(s) required for autophagy, we identified a novel ORF, ATG29/YPL166w. atg29{delta} cells were sensitive to starvation and induction of autophagy was severely retarded. However, the Cvt pathway operated normally. Therefore, ATG29 is an ATG gene specifically required for autophagy. Additionally, an Atg29-GFP fusion protein was observed to localize to the PAS. From these results, we propose that Atg29 functions in autophagosome formation at the PAS in collaboration with other Atg proteins.
- OSTI ID:
- 20793246
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 338, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2005.10.163; PII: S0006-291X(05)02441-1; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
Similar Records
Kibra and aPKC regulate starvation-induced autophagy in Drosophila
In vivo effect of an antilipolytic drug (3,5'-dimethylpyrazole) on autophagic proteolysis and autophagy-related gene expression in rat liver