GRP94 in ER quality control and stress responses

Semin Cell Dev Biol. 2010 Jul;21(5):479-85. doi: 10.1016/j.semcdb.2010.03.004. Epub 2010 Mar 16.


A system of endoplasmic reticulum (ER) chaperones has evolved to optimize the output of properly folded secretory and membrane proteins. An important player in this network is Glucose Regulated Protein 94 (GRP94). Over the last decade, new structural and functional data have begun to delineate the unique characteristics of GRP94 and have solidified its importance in ER quality control pathways. This review describes our current understanding of GRP94 and the four ways in which it contributes to the ER quality control: (1) chaperoning the folding of proteins; (2) interacting with other components of the ER protein folding machinery; (3) storing calcium; and (4) assisting in the targeting of malfolded proteins to ER-associated degradation (ERAD).

Publication types

  • Review

MeSH terms

  • Animals
  • Endoplasmic Reticulum / metabolism*
  • Endoplasmic Reticulum / physiology*
  • HSP70 Heat-Shock Proteins
  • Membrane Proteins / metabolism
  • Molecular Chaperones / metabolism
  • Protein Folding
  • Protein Processing, Post-Translational
  • Proteins / metabolism


  • HSP70 Heat-Shock Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • Proteins
  • glucose-regulated proteins