Structural transitions modulate the chaperone activities of Grp94

Trends Biochem Sci. 2024 Sep;49(9):752-753. doi: 10.1016/j.tibs.2024.06.007. Epub 2024 Jun 20.

Abstract

A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94.

Keywords: BiP; DEER; Grp94; Hsp90; endoplasmic reticulum (ER); protein folding.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Endoplasmic Reticulum / metabolism
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism
  • Molecular Chaperones* / chemistry
  • Molecular Chaperones* / metabolism

Substances

  • endoplasmin
  • Molecular Chaperones
  • Membrane Glycoproteins
  • Adenosine Triphosphate