Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts
The ubiquitin-proteasome system (UPS) is the preeminent proteolytic system in eukaryotes. While soluble nucleocytosolic proteins are readily accessed by the UPS, organelle-localised proteins present major, membrane-related accessibility challenges. Cells overcome this problem by employing the conserved AAA+ ATPase Cdc48 to extract organellar proteins to the cytosol, thereby enabling proteasomal degradation. Major Cdc48-dependent proteolytic systems exist at the endoplasmic reticulum, mitochondria and chloroplasts, and are uniquely adapted to deliver protein homeostasis within the respective organelles. We provide a focused comparison of these systems, analysing similarities and differences between them. Better understanding of underlying principles has important implications spanning human health and agriculture.
Authors
- Sreedhar Nellaepalli (ORCID: https://orcid.org/0000-0002-9402-6951)
- Anne Lau
- Paul Jarvis (ORCID: https://orcid.org/0000-0003-2127-5671)
Institutions
- University of Oxford (GB)
Publication Details
- Journal
- Nature Communications
- Published
- 2026-07-02
- DOI
- https://doi.org/10.1038/s41467-026-74728-z
- Primary Topic
- Ubiquitin and proteasome pathways
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- UK Research and Innovation
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council