Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 21, Issue 5, Pages 479-485Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2010.03.004
Keywords
ER chaperone; HSP90; IGF; Calcium; ERAD
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Funding
- NIA NIH HHS [R01 AG018001] Funding Source: Medline
- NIGMS NIH HHS [R01 GM077480, T32 GM008275] Funding Source: Medline
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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). (c) 2010 Elsevier Ltd. All rights reserved.
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