Abstract：
: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).
journal_name
Semin Cell Dev Bioljournal_title
Seminars in cell & developmental biologyauthors
Eletto D,Dersh D,Argon Ydoi
10.1016/j.semcdb.2010.03.004subject
Has Abstractpub_date
2010-07-01 00:00:00pages
479-85issue
5eissn
1084-9521issn
1096-3634pii
S1084-9521(10)00057-1journal_volume
21pub_type
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