TECPR1 conjugates LC3 to damaged endomembranes upon detection of sphingomyelin exposure

Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by...

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Vydané v:The EMBO journal Ročník 42; číslo 17; s. e113012 - n/a
Hlavní autori: Boyle, Keith B, Ellison, Cara J, Elliott, Paul R, Schuschnig, Martina, Grimes, Krista, Dionne, Marc S, Sasakawa, Chihiro, Munro, Sean, Martens, Sascha, Randow, Felix
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: London Nature Publishing Group UK 04.09.2023
Springer Nature B.V
John Wiley and Sons Inc
Predmet:
Animals
ATG5‐ATG12 E3 ligase
Autophagy
Autophagy-Related Protein 5 - metabolism
Autophagy-Related Proteins - metabolism
Bacteria
Carrier Proteins - metabolism
Cellular stress response
Conjugation
Crystal structure
Crystallography
Cytosol
Damage detection
DysF
EMBO07
EMBO20
Exposure
Life Sciences
Lipids
Mammals
membrane damage
Membranes
Microtubule-Associated Proteins - metabolism
Polysaccharides
Receptors
Sphingomyelin
Sphingomyelins
Tryptophan
Ubiquitin
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
Vacuoles
DysF
sphingomyelin
autophagy
membrane damage
ATG5‐ATG12 E3 ligase
ATG5-ATG12 E3 ligase
ISSN:0261-4189, 1460-2075, 1460-2075
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Abstract Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin‐8 triggers anti‐bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta‐propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N‐terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent‐exposed tryptophan (W154) essential for binding to sphingomyelin‐positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12‐E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin‐specific TECPR1, in an arrangement reminiscent of certain multi‐subunit ubiquitin E3 ligases. Synopsis Upon damage to bacteria‐containing vacuoles sphingomyelin transits from the luminal to the cytosolic face of the membrane. Here we show that TECPR1 detects cytosolically exposed sphingomyelin and directs conjugation of the autophagy effector protein LC3 to those membranes. TECPR1 is a novel danger receptor that detects sphingomyelin exposed on the cytosolic face of damaged membranes. The N‐terminal DysF domain of TECPR1 binds sphingomyelin and recruits TECPR1 to damaged membranes. TECPR1 recruits ATG5 to sphingomyelin‐positive membranes. The TECPR1‐ATG5‐ATG12 complex is a sphingomyelin‐activated E3 ligase catalyzing the lipid conjugation of LC3. Graphical Abstract TECPR1 detects cytosolically‐exposed sphingomyelin and recruits ATG5/ATG12‐E3 ligase to damaged membranes to mediate lipid conjugation of LC3 independently of ATG16L.
AbstractList Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin-8 triggers anti-bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta-propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N-terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent-exposed tryptophan (W154) essential for binding to sphingomyelin-positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12-E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin-specific TECPR1, in an arrangement reminiscent of certain multi-subunit ubiquitin E3 ligases.Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin-8 triggers anti-bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta-propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N-terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent-exposed tryptophan (W154) essential for binding to sphingomyelin-positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12-E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin-specific TECPR1, in an arrangement reminiscent of certain multi-subunit ubiquitin E3 ligases.
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin‐8 triggers anti‐bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta‐propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N‐terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent‐exposed tryptophan (W154) essential for binding to sphingomyelin‐positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12‐E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin‐specific TECPR1, in an arrangement reminiscent of certain multi‐subunit ubiquitin E3 ligases. Synopsis Upon damage to bacteria‐containing vacuoles sphingomyelin transits from the luminal to the cytosolic face of the membrane. Here we show that TECPR1 detects cytosolically exposed sphingomyelin and directs conjugation of the autophagy effector protein LC3 to those membranes. TECPR1 is a novel danger receptor that detects sphingomyelin exposed on the cytosolic face of damaged membranes. The N‐terminal DysF domain of TECPR1 binds sphingomyelin and recruits TECPR1 to damaged membranes. TECPR1 recruits ATG5 to sphingomyelin‐positive membranes. The TECPR1‐ATG5‐ATG12 complex is a sphingomyelin‐activated E3 ligase catalyzing the lipid conjugation of LC3. TECPR1 detects cytosolically‐exposed sphingomyelin and recruits ATG5/ATG12‐E3 ligase to damaged membranes to mediate lipid conjugation of LC3 independently of ATG16L.
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin-8 triggers anti-bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta-propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N-terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent-exposed tryptophan (W154) essential for binding to sphingomyelin-positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12-E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin-specific TECPR1, in an arrangement reminiscent of certain multi-subunit ubiquitin E3 ligases.
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin‐8 triggers anti‐bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta‐propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N‐terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent‐exposed tryptophan (W154) essential for binding to sphingomyelin‐positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12‐E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin‐specific TECPR1, in an arrangement reminiscent of certain multi‐subunit ubiquitin E3 ligases. image Upon damage to bacteria‐containing vacuoles sphingomyelin transits from the luminal to the cytosolic face of the membrane. Here we show that TECPR1 detects cytosolically exposed sphingomyelin and directs conjugation of the autophagy effector protein LC3 to those membranes. TECPR1 is a novel danger receptor that detects sphingomyelin exposed on the cytosolic face of damaged membranes. The N‐terminal DysF domain of TECPR1 binds sphingomyelin and recruits TECPR1 to damaged membranes. TECPR1 recruits ATG5 to sphingomyelin‐positive membranes. The TECPR1‐ATG5‐ATG12 complex is a sphingomyelin‐activated E3 ligase catalyzing the lipid conjugation of LC3.
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin‐8 triggers anti‐bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta‐propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N‐terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent‐exposed tryptophan (W154) essential for binding to sphingomyelin‐positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12‐E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin‐specific TECPR1, in an arrangement reminiscent of certain multi‐subunit ubiquitin E3 ligases. Synopsis Upon damage to bacteria‐containing vacuoles sphingomyelin transits from the luminal to the cytosolic face of the membrane. Here we show that TECPR1 detects cytosolically exposed sphingomyelin and directs conjugation of the autophagy effector protein LC3 to those membranes. TECPR1 is a novel danger receptor that detects sphingomyelin exposed on the cytosolic face of damaged membranes. The N‐terminal DysF domain of TECPR1 binds sphingomyelin and recruits TECPR1 to damaged membranes. TECPR1 recruits ATG5 to sphingomyelin‐positive membranes. The TECPR1‐ATG5‐ATG12 complex is a sphingomyelin‐activated E3 ligase catalyzing the lipid conjugation of LC3. Graphical Abstract TECPR1 detects cytosolically‐exposed sphingomyelin and recruits ATG5/ATG12‐E3 ligase to damaged membranes to mediate lipid conjugation of LC3 independently of ATG16L.
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin‐8 triggers anti‐bacterial autophagy, but how cells sense and respond to cytosolically exposed sphingomyelin remains unknown. Here, we identify TECPR1 (tectonin beta‐propeller repeat containing 1) as a receptor for cytosolically exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N‐terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solving the crystal structure of N'DysF, we identified key residues required for the interaction, including a solvent‐exposed tryptophan (W154) essential for binding to sphingomyelin‐positive membranes and the conjugation of LC3 to lipids. Specificity of the ATG5/ATG12‐E3 ligase responsible for the conjugation of LC3 is therefore conferred by interchangeable receptor subunits, that is, the canonical ATG16L1 and the sphingomyelin‐specific TECPR1, in an arrangement reminiscent of certain multi‐subunit ubiquitin E3 ligases. TECPR1 detects cytosolically‐exposed sphingomyelin and recruits ATG5/ATG12‐E3 ligase to damaged membranes to mediate lipid conjugation of LC3 independently of ATG16L.
Author Randow, Felix
Boyle, Keith B
Grimes, Krista
Sasakawa, Chihiro
Ellison, Cara J
Dionne, Marc S
Munro, Sean
Elliott, Paul R
Schuschnig, Martina
Martens, Sascha
AuthorAffiliation 6 Center for Molecular Biology, Department of Biochemistry and Cell Biology University of Vienna Vienna Austria
8 Present address: Department of Biochemistry University of Oxford Oxford UK
2 Max Perutz Labs, Vienna BioCenter (VBC) University of Vienna Vienna Austria
7 Department of Medicine, Addenbrooke's Hospital University of Cambridge Cambridge UK
5 Nippon Institute for Biological Science Ome Japan
4 Medical Mycology Research Center Chiba University Chiba Japan
1 Division of Protein and Nucleic Acid Chemistry MRC Laboratory of Molecular Biology Cambridge UK
3 MRC Centre for Molecular Bacteriology and Infection Imperial College London London UK
AuthorAffiliation_xml – name: 8 Present address: Department of Biochemistry University of Oxford Oxford UK
– name: 4 Medical Mycology Research Center Chiba University Chiba Japan
– name: 6 Center for Molecular Biology, Department of Biochemistry and Cell Biology University of Vienna Vienna Austria
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– name: 7 Department of Medicine, Addenbrooke's Hospital University of Cambridge Cambridge UK
– name: 1 Division of Protein and Nucleic Acid Chemistry MRC Laboratory of Molecular Biology Cambridge UK
– name: 2 Max Perutz Labs, Vienna BioCenter (VBC) University of Vienna Vienna Austria
– name: 5 Nippon Institute for Biological Science Ome Japan
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  surname: Boyle
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  email: kboyle@mrc-lmb.cam.ac.uk
  organization: Division of Protein and Nucleic Acid Chemistry, MRC Laboratory of Molecular Biology
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  surname: Ellison
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  organization: Division of Protein and Nucleic Acid Chemistry, MRC Laboratory of Molecular Biology, Department of Biochemistry, University of Oxford
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  surname: Elliott
  fullname: Elliott, Paul R
  organization: Division of Protein and Nucleic Acid Chemistry, MRC Laboratory of Molecular Biology, Department of Biochemistry, University of Oxford
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  surname: Schuschnig
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  organization: Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna
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  orcidid: 0000-0003-3786-8199
  surname: Martens
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/37409490$$D View this record in MEDLINE/PubMed
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ISSN 0261-4189
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Issue 17
Keywords DysF
sphingomyelin
autophagy
membrane damage
ATG5‐ATG12 E3 ligase
ATG5-ATG12 E3 ligase
Language English
License Attribution
2023 MRC Laboratory of Molecular Biology and The Authors. Published under the terms of the CC BY 4.0 license.
This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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Snippet Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria‐containing vacuoles (BCVs) and subsequent rupture of the BCV membrane,...
Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane,...
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wiley
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SourceType Open Access Repository
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Enrichment Source
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StartPage e113012
SubjectTerms Animals
ATG5‐ATG12 E3 ligase
Autophagy
Autophagy-Related Protein 5 - metabolism
Autophagy-Related Proteins - metabolism
Bacteria
Carrier Proteins - metabolism
Cellular stress response
Conjugation
Crystal structure
Crystallography
Cytosol
Damage detection
DysF
EMBO07
EMBO20
Exposure
Life Sciences
Lipids
Mammals
membrane damage
Membranes
Microtubule-Associated Proteins - metabolism
Polysaccharides
Receptors
Sphingomyelin
Sphingomyelins
Tryptophan
Ubiquitin
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - metabolism
Vacuoles
Title TECPR1 conjugates LC3 to damaged endomembranes upon detection of sphingomyelin exposure
URI https://link.springer.com/article/10.15252/embj.2022113012
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembj.2022113012
https://www.ncbi.nlm.nih.gov/pubmed/37409490
https://www.proquest.com/docview/2860290142
https://www.proquest.com/docview/2834000426
https://pubmed.ncbi.nlm.nih.gov/PMC10476172
Volume 42
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