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Atg15 is a vacuolar phospholipase that disintegrates organelle membranes
Open accessPreprint — published as 10.1016/j.celrep.2023.113567 · Paper page
Abstract
Summary: 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 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 that in acidic environments digests phospholipid to generate lysophospholipid and free fatty acid. The activity of CtAtg15(73–475) was markedly elevated by limited digestion with proteinase K. Proteinase K–treated CtAtg15(73–475) was detected as three fragments, with cleavage between S159 and V160, and between F209 and N210. We inserted the human rhinovirus 3C protease recognition sequence into the two sites and found that cleavage between S159 and V160 was important to activate CtAtg15(73–475). We confirmed that CtAtg15 compensated for the absence of ATG15 in Saccharomyces cerevisiae cells, indicating that CtAtg15 could disintegrate S. cerevisiae IAC in vivo . Further, both mitochondria and IAC were disintegrated by CtAtg15 in S. cerevisiae . This study suggests that Atg15 can degrade any organelle membrane, indicating that Atg15 plays a role in disrupting organelle membranes delivered to vacuoles by autophagy.
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Metadata
- Authors
- Watanabe, Y., Iwasaki, Y., Sasaki, K., & Suzuki, K.
- Affiliations
- Yamagata University (JP)
- The University of Tokyo (JP)
- Collaborative Research Institute for Innovative Microbiology, The University of Tokyo (JP)
- Corresponding author
- Watanabe, Yasunori
- Suzuki, Kuninori
- Venue
- Cell Reports
- Publisher
- openRxiv
- Published
- 2023-06-01
- Volume
- 42
- Issue
- 12
- Pages
- 113567-113567
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W4389955954
- Cited by
- 17
- References
- 1
- 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
- Locations
- Cell Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
- PubMed (publishedVersion)
- Funders
- Naito Foundation
- Japan Agency for Medical Research and Development (23ama121029j0002)
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for the Promotion of Science (22H02569, 22K06096, 23K11313, 21K19205, 20H05313, 23K23833, 21H03551)
- Japan Science and Technology Agency (JP201032912)
- Core Research for Evolutional Science and Technology
- 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., & Suzuki, K. (2023). Atg15 is a vacuolar phospholipase that disintegrates organelle membranes. Cell Reports. https://doi.org/10.1101/2023.05.31.543165
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