Protein-protein interactions of ER-resident selenoproteins with their physiological partners

Biochimie. 2020 Apr-May:171-172:197-204. doi: 10.1016/j.biochi.2020.03.012. Epub 2020 Mar 15.

Abstract

ER is a highly specialized complex of branched microtubules enclosed in a membrane and communicating with each other, its functions in the cell are important and very diverse: lipid and phospholipid synthesis, calcium storage, hormone synthesis, protein synthesis and maturation, membrane production, toxin neutralization, etc. The high concentration of calcium ions and the oxidizing properties of the contents of the ER cavities contribute to the proper synthesis and folding of proteins designed for secretion or exposure on the surface of the cell membrane. However, disturbance of redox regulation can lead to the accumulation of improperly folded proteins in the ER, disruption of calcium regulation, which can cause ER-stress. This review is devoted to the role of ER-resident selenoproteins in the processes occurring in this organelle of a cell. The main emphasis is placed on the study of protein-protein interactions of selenoproteins with their physiological partners; this will facilitate understanding of their functional purpose in this organelle. Currently, 7 selenoproteins are known that are localized in the ER, but the functions of most of them are not at all clear, for some, physiological partners have been identified. It is known that selenoproteins are oxidoreductases with antioxidant properties, this is extremely important for the normal functioning of ER. Therefore, this review can be very useful for understanding the full picture of the functions of ER-resident selenoproteins obtained on the basis of recent data.

Keywords: ER–Resident selenoproteins; Protein–protein interactions.

Publication types

  • Review

MeSH terms

  • Animals
  • Antioxidants / metabolism
  • Calcium / metabolism
  • Cell Line, Tumor
  • Drosophila melanogaster
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum Stress*
  • Humans
  • Mice
  • Oxidation-Reduction
  • Proteolysis
  • Selenoproteins / metabolism*

Substances

  • Antioxidants
  • Selenoproteins
  • Calcium