Ubiquitin-proteasome signaling in lung injury

Transl Res. 2018 Aug:198:29-39. doi: 10.1016/j.trsl.2018.04.003. Epub 2018 Apr 23.

Abstract

Cell homeostasis requires precise coordination of cellular proteins function. Ubiquitination is a post-translational modification that modulates protein half-life and function and is tightly regulated by ubiquitin E3 ligases and deubiquitinating enzymes. Lung injury can progress to acute respiratory distress syndrome that is characterized by an inflammatory response and disruption of the alveolocapillary barrier resulting in alveolar edema accumulation and hypoxemia. Ubiquitination plays an important role in the pathobiology of acute lung injury as it regulates the proteins modulating the alveolocapillary barrier and the inflammatory response. Better understanding of the signaling pathways regulated by ubiquitination may lead to novel therapeutic approaches by targeting specific elements of the ubiquitination pathways.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Humans
  • Lung Injury / enzymology*
  • Proteasome Endopeptidase Complex / metabolism*
  • Proteolysis
  • Respiratory Distress Syndrome / enzymology*
  • Signal Transduction*
  • Ubiquitin / metabolism*

Substances

  • Ubiquitin
  • Proteasome Endopeptidase Complex