The Dsc ubiquitin ligase complex identifies transmembrane degrons to degrade orphaned proteins at the Golgi.

Golgi Apparatus / metabolism Saccharomyces cerevisiae Proteins / metabolism Saccharomyces cerevisiae / metabolism Membrane Proteins / metabolism Proteolysis Endosomal Sorting Complexes Required for Transport / metabolism Protein Transport Endoplasmic Reticulum / metabolism Ubiquitin-Protein Ligases / metabolism Glycerophospholipids / metabolism Degrons

Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
26 Oct 2024
Historique:
received: 24 03 2024
accepted: 16 10 2024
medline: 27 10 2024
pubmed: 27 10 2024
entrez: 27 10 2024
Statut: epublish

Résumé

The Golgi apparatus is essential for protein sorting, yet its quality control mechanisms are poorly understood. Here we show that the Dsc ubiquitin ligase complex uses its rhomboid pseudo-protease subunit, Dsc2, to assess the hydrophobic length of α-helical transmembrane domains (TMDs) at the Golgi. Thereby the Dsc complex likely interacts with orphaned ER and Golgi proteins that have shorter TMDs and ubiquitinates them for targeted degradation. Some Dsc substrates will be extracted by Cdc48 for endosome and Golgi associated proteasomal degradation (EGAD), while others will undergo ESCRT dependent vacuolar degradation. Some substrates are degraded by both, EGAD- or ESCRT pathways. The accumulation of Dsc substrates entails a specific increase in glycerophospholipids with shorter and asymmetric fatty acyl chains. Hence, the Dsc complex mediates the selective degradation of orphaned proteins at the sorting center of cells, which prevents their spreading across other organelles and thereby preserves cellular membrane protein and lipid composition.

Identifiants

DOI: 10.1038/s41467-024-53676-6 PMID: 39461958
pubmed: 39461958
doi: 10.1038/s41467-024-53676-6
pii: 10.1038/s41467-024-53676-6
doi:

Substances chimiques

Saccharomyces cerevisiae Proteins 0
Membrane Proteins 0
Endosomal Sorting Complexes Required for Transport 0
Ubiquitin-Protein Ligases EC 2.3.2.27
Glycerophospholipids 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

9257

Subventions

Organisme : Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung)
ID : 10.55776/P32161
Organisme : Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung)
ID : 10.55776/P34907
Organisme : Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung)
ID : 10.55776/DOC82
Organisme : Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung)
ID : 10.55776/P36187
Organisme : Fonds National de la Recherche Luxembourg (National Research Fund)
ID : 13571826
Organisme : EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)
ID : 847681

Informations de copyright

© 2024. The Author(s).

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Auteurs

Yannick Weyer (Y)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0000-0002-2612-6774

Sinead I Schwabl (SI)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Xuechen Tang (X)

Department of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck, University of Innsbruck, Innsbruck, Austria.

Astha Purwar (A)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Konstantin Siegmann (K)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Angela Ruepp (A)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0000-0001-5436-6030

Theresia Dunzendorfer-Matt (T)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0000-0002-1315-6317

Michael A Widerin (MA)

Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Veronika Niedrist (V)

Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.

Noa J M Mutsters (NJM)

Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0009-0001-4051-9638

Maria G Tettamanti (MG)

Department of Molecular and Cell Biology, University of Geneva, Geneva, Switzerland.
Department of Biochemistry, University of Geneva, Geneva, Switzerland.

Sabine Weys (S)

Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
Institute of Science and Technology Austria (ISTA), Am Campus 1, Klosterneuburg, Austria.

Bettina Sarg (B)

Institute of Medical Biochemistry, Protein Core Facility, Medical University of Innsbruck, Innsbruck, Austria.

Leopold Kremser (L)

Institute of Medical Biochemistry, Protein Core Facility, Medical University of Innsbruck, Innsbruck, Austria.

Klaus R Liedl (KR)

Institute of Medical Biochemistry, Protein Core Facility, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0000-0002-0985-2299

Oliver Schmidt (O)

Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria.
ORCID: 0000-0002-7921-4663

David Teis (D)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria. david.teis@i-med.ac.at.
Institute of Cell Biology, Biocenter, Medical University of Innsbruck, Innsbruck, Austria. david.teis@i-med.ac.at.
ORCID: 0000-0002-8181-0253

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Classifications MeSH

questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Appareil de Golgi › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Métabolisme › Protéolyse › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines du transport vésiculaire › Complexes de tri endosomique requis pour le transport › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Métabolisme › Transport biologique › Transport des protéines › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Réticulum endoplasmique › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › The Dsc ubiquitin ligase complex identifies...
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › The Dsc ubiquitin ligase complex identifies...