The Dsc complex and its role in Golgi quality control.

Golgi quality control ubiquitin

Journal

Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897

Informations de publication

Date de publication:
26 Sep 2024
Historique:
received: 26 07 2024
revised: 20 08 2024
accepted: 27 08 2024
medline: 26 9 2024
pubmed: 26 9 2024
entrez: 26 9 2024
Statut: aheadofprint

Résumé

Membrane proteins play crucial roles in cellular functions. However, processes such as the insertion of membrane proteins into the endoplasmic reticulum (ER), their folding into native structures, the assembly of multi-subunit membrane protein complexes, and their targeting from the ER to specific organelles are prone to errors and have a relatively high failure rate. To prevent the accumulation of defective or orphaned membrane proteins, quality control mechanisms assess folding, quantity, and localization of these proteins. This quality control is vital for preserving organelle integrity and maintaining cellular health. In this mini-review, we will focus on how selective membrane protein quality control at the Golgi apparatus, particularly through the defective for SREBP cleavage (Dsc) ubiquitin ligase complex, detects orphaned proteins and prevents their mis-localization to other organelles.

Identifiants

pubmed: 39324639
pii: 235011
doi: 10.1042/BST20230375
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2024 The Author(s).

Auteurs

Yannick Weyer (Y)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

David Teis (D)

Institute of Molecular Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.

Classifications MeSH