PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation

EMBO Rep. 2009 Feb;10(2):173-9. doi: 10.1038/embor.2008.238. Epub 2009 Jan 16.

Abstract

Ubiquilins (UBQLNs) are adaptor proteins thought to deliver ubiquitinated substrates to proteasomes. Here, we show a role for UBQLN in autophagy: enforced expression of UBQLN protects cells from starvation-induced death, whereas depletion of UBQLN renders cells more susceptible. The UBQLN protective effect requires the autophagy-related genes ATG5 and ATG7, two essential components of autophagy. The ubiquitin-associated domain of UBQLN mediates both its association with autophagosomes and its protective effect against starvation. Depletion of UBQLN delays the delivery of autophagosomes to lysosomes. This study identifies a new role for UBQLN in regulating the maturation of autophagy, expanding the involvement of ubiquitin-related proteins in this process.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport / antagonists & inhibitors
  • Adaptor Proteins, Vesicular Transport / genetics
  • Adaptor Proteins, Vesicular Transport / physiology
  • Animals
  • Autophagy / drug effects
  • Autophagy / physiology*
  • Autophagy-Related Protein 5
  • Autophagy-Related Protein 7
  • Autophagy-Related Proteins
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / physiology*
  • Culture Media / pharmacology
  • HeLa Cells / cytology
  • HeLa Cells / drug effects
  • Humans
  • Mice
  • Microscopy, Immunoelectron
  • Microtubule-Associated Proteins / antagonists & inhibitors
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism
  • Microtubule-Associated Proteins / physiology
  • Phagosomes / metabolism
  • Protein Interaction Mapping
  • Protein Structure, Tertiary
  • RNA Interference
  • RNA, Small Interfering / physiology
  • Recombinant Fusion Proteins / antagonists & inhibitors
  • Recombinant Fusion Proteins / physiology
  • Ubiquitin-Activating Enzymes / antagonists & inhibitors
  • Ubiquitin-Activating Enzymes / genetics
  • Ubiquitin-Activating Enzymes / physiology
  • Ubiquitins / antagonists & inhibitors
  • Ubiquitins / genetics
  • Ubiquitins / physiology*

Substances

  • ATG5 protein, human
  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • Autophagy-Related Protein 5
  • Autophagy-Related Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Culture Media
  • MAP1LC3A protein, human
  • Microtubule-Associated Proteins
  • RNA, Small Interfering
  • Recombinant Fusion Proteins
  • UBQLN1 protein, human
  • UBQLN1 protein, mouse
  • UBQLN2 protein, human
  • UBQLN2 protein, mouse
  • Ubiquitins
  • ATG7 protein, human
  • Autophagy-Related Protein 7
  • Ubiquitin-Activating Enzymes