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<p>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+&#xa0;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.</p>

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Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年7月2日

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  • Anne Sophie Lau,
  • Sreedhar Nellaepalli,
  • R. Paul Jarvis

摘要

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.