Interplay among oxidative stress, redox signaling, er stress, autophagy, and protein ubiquitylation in cardiometabolic disorders

Taixing Cui, Xuejun Wang

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Normal function of proteins is essential to all aspects of life. Attaining and maintaining the proper folding of a protein is required for normal functioning of the protein. As the intracellular and extracellular stresses (e.g., oxidative stress) can cause protein malfolding (both misfolding and unfolding) and deployment of a misfolded protein could be catastrophic, the cell has developed an elaborate network of molecular chaperones and targeted protein degradation pathways including the proteasomal degradation pathway and the autophagy to minimize the level and the toxicity of malfolded proteins in the cell. This set of intertwined mechanisms is known as protein quality control (PQC). This chapter focuses on an emerging role of ubiquitylation in regulating PQC-associated protein degradation in the setting of oxidative and endoplasmic reticulum stresses associated with cardiometabolic diseases.

Original languageEnglish (US)
Title of host publicationAutophagy and Cardiometabolic Diseases
Subtitle of host publicationFrom Molecular Mechanisms to Translational Medicine
PublisherElsevier
Pages29-42
Number of pages14
ISBN (Electronic)9780128052532
ISBN (Print)9780128054420
DOIs
StatePublished - Jan 1 2018

Keywords

  • Autophagy
  • Er stress
  • Metabolic syndrome
  • Oxidative stress
  • Protein quality control
  • Ubiquitylation

ASJC Scopus subject areas

  • Medicine(all)

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  • Cite this

    Cui, T., & Wang, X. (2018). Interplay among oxidative stress, redox signaling, er stress, autophagy, and protein ubiquitylation in cardiometabolic disorders. In Autophagy and Cardiometabolic Diseases: From Molecular Mechanisms to Translational Medicine (pp. 29-42). Elsevier. https://doi.org/10.1016/B978-0-12-805253-2.00003-1