The roles of cytosolic quality control proteins, SGTA and the BAG6 complex, in disease

Rashi Benarroch, Jennifer M. Austin, Fahmeda Ahmed, Rivka L. Isaacson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)

Abstract

SGTA is a co-chaperone that, in collaboration with the complex of BAG6/UBL4A/TRC35, facilitates the biogenesis and quality control of hydrophobic proteins, protecting them from the aqueous cytosolic environment. This work includes targeting tail-anchored proteins to their resident membranes, sorting of membrane and secretory proteins that mislocalize to the cytoplasm and endoplasmic reticulum-associated degradation of misfolded proteins. Since these functions are all vital for the cell's continued proteostasis, their disruption poses a threat to the cell, with a particular risk of protein aggregation, a phenomenon that underpins many diseases. Although the specific disease implications of machinery involved in quality control of hydrophobic substrates are poorly understood, here we summarize much of the available information on this topic.

Original languageEnglish
JournalAdvances in Protein Chemistry and Structural Biology
DOIs
Publication statusE-pub ahead of print - 18 Dec 2018

Keywords

  • BAG6
  • Chaperones
  • Co-chaperones
  • Hydrophobic proteins
  • Proteostasis
  • Quality control
  • SGTA
  • Tail-anchored proteins
  • TRC35
  • UBL4A

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