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Atg15 is a vacuolar phospholipase that disintegrates organelle membranes
Open accessPublished version of a preprint
Abstract
Atg15 (autophagy-related 15) is a vacuolar phospholipase essential for the degradation of cytoplasm-to-vacuole targeting (Cvt) bodies and autophagic bodies, hereinafter referred to as intravacuolar/intralysosomal autophagic compartments (IACs), but it remains unknown if Atg15 directly disrupts IAC membranes. Here, we show that the recombinant Chaetomium thermophilum Atg15 lipase domain (CtAtg15(73–475)) possesses phospholipase activity. The activity of CtAtg15(73–475) was markedly elevated by limited digestion. We inserted the human rhinovirus 3C protease recognition sequence and found that cleavage between S159 and V160 was important to activate CtAtg15(73–475). Our molecular dynamics simulation suggested that the cleavage facilitated conformational change around the active center of CtAtg15, resulting in an exposed state. We confirmed that CtAtg15 could disintegrate S. cerevisiae IAC in vivo . Further, both mitochondria and IAC of S. cerevisiae were disintegrated by CtAtg15. This study suggests Atg15 plays a role in disrupting any organelle membranes delivered to vacuoles by autophagy.
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Research works printed but not linked: 1
- Suzuki, 2002, Studies of cargo delivery to the vacuole mediated by autophagosomes in Saccharomyces cerevisiae, Dev. Cell, 3, 815, 10.1016/S1534-5807(02)00359-3 · DOI
Metadata
- Authors
- Watanabe, Y., Iwasaki, Y., Sasaki, K., Motono, C., Imai, K., & Suzuki, K.
- Affiliations
- Yamagata University (JP)
- The University of Tokyo (JP)
- Waseda University (JP)
- Global Research and Development Center for Business by Quantum-AI technology (JP)
- Collaborative Research Institute for Innovative Microbiology, The University of Tokyo (JP)
- Corresponding author
- Watanabe, Yasunori
- Suzuki, Kuninori
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2023-12
- Volume
- 42
- Issue
- 12
- Pages
- 113567
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W4389955954
- Cited by
- 17
- References
- 50
- Citations by year
- 2026: 9 · 2025: 5 · 2024: 3
- FWCI
- 3.39
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/4.0/ (vor)
- Locations
- Cell Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (20H05313, 21H03551, 21K19205, 22H02569, 22K06096, 23K11313)
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Science and Technology Agency (JP201032912)
- Core Research for Evolutional Science and Technology
- Japan Agency for Medical Research and Development (23ama121029j0002)
- Naito Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- autophagy, Chaetomium thermophilum, proteolytic activation, conformational change, mitochondrial degradation, Saccharomyces cerevisiae
- MeSH terms
- Protein Domains, Autophagy, Chaetomium, Enzyme Activation, Fungal Proteins, Humans, Intracellular Membranes, Lipase, Mitochondria, Models, Molecular, Phospholipases, Recombinant Proteins, Saccharomyces cerevisiae, Vacuoles, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins, Molecular Dynamics Simulation
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- Watanabe, Y., Iwasaki, Y., Sasaki, K., Motono, C., Imai, K., & Suzuki, K. (2023). Atg15 is a vacuolar phospholipase that disintegrates organelle membranes. Cell Reports. https://doi.org/10.1016/j.celrep.2023.113567
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