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. Author manuscript; available in PMC: 2007 Oct 23.
Published in final edited form as: FEBS Lett. 2007 Apr 25;581(19):3641–3651. doi: 10.1016/j.febslet.2007.04.045

Table 2.

Summary of function and disease relevance of ER chaperones, co-chaperones and folding enzymes

Protein Localization Function Knockout mouse model Diseases Reference
Calnexin ER transmembrane
Cell surface
Chaperone, glycoprotein folding Postnatal death and motor disorders Alzheimer’s disease [46,57,93]
Calreticulin ER lumen
Cytosol
Cell surface
Chaperone, glycoprotein folding, Ca2+-binding Embryonic lethality at E14.5 due to defective embryonic cardiac development Cardiac hypertrophy
Alzheimer’s disease
Autoimmune diseases
[36,91,131,133,134]
EDEM ER lumen Chaperone, recognition and targeting of unfolded glycoprotein for degradation N.D. N.D. [30]
ERp72 ER lumen Thio-oxidoreductase to catalyze disulfide bond formation N.D. N.D. [135]
Herp ER transmembrane Ubiquitin-like protein involved in ERAD N.D. Atherosclerosis
Alzheimer’s disease
[109,136,137]
P58IPK Cytosol
ER membrane
Co-chaperone, negative regulator of eIF2α kinase PERK and PKR, cotranslocational degradation Development of diabetes associated with increased β-cell death Diabetes (mouse) [22,23,25,118,119]
UGGT ER lumen Glucosyltransferase, recognition of misfolded glycoprotein and reglucosylation of N-glycan Embryonic lethality at E13 N.D. [37]