GRP94 in ER quality control and stress responses

D Eletto, D Dersh, Y Argon - Seminars in cell & developmental biology, 2010 - Elsevier
Seminars in cell & developmental biology, 2010Elsevier
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 …
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).
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