Calnexin/CANX is a single-pass type I membrane protein which belongs to the calreticulin family. It consists of a large N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail. The function of calnexin is to retain unfolded or unassembled N-linked glycoproteins in the endoplasmic reticulum. Calnexin is a calcium-binding protein that interacts briefly with newly synthesized glycoproteins in the endoplasmic reticulum. Calnexin may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. Calnexin seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.
Calreticulin is a multifunctional protein. It acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin binds Ca2+ ions (a second messenger in signal transduction); rendering it inactive. The Ca2+ is bound with low affinity; but high capacity; and can be released on a signal. Located in storage compartments associated with the endoplasmic reticulum; calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo; as well as retinoic acid-induced neuronal differentiation. Therefore; calreticulin acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.
Calreticulin-3 belongs to the calreticulin family, members of which are calcium binding chaperones localized mainly in the endoplasmic reticulum. It can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. During spermatogenesis process, Calreticulin-3 may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Defects in CALR3 are the cause of familial hypertrophic cardiomyopathy type 19 (CMH19), it is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain.
Calreticulin is a multifunctional protein. It acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin binds Ca2+ ions (a second messenger in signal transduction), rendering it inactive. The Ca2+ is bound with low affinity, but high capacity, and can be released on a signal. Located in storage compartments associated with the endoplasmic reticulum, calreticulin also binds to misfolded proteins and prevents them from being exported from the endoplasmic reticulum to the golgi apparatus. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, calreticulin acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.
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