Calreticulin is an ER resident protein that buffers Ca2+ and participates in the folding of newly synthesized proteins and glycoproteins. The lumen of the ER contains many proteins which carry out these diverse functions. The endoplasmic reticulum (ER)1 plays a critical role in many cellular processes, including Ca2+ storage and release, lipid synthesis, and protein synthesis, folding, and post-translational modification. The calreticulin-deficient mouse and cardiac pathology Structure/function relationships in calnexin and calreticulin The calreticulin/calnexin cycle and ER quality control Calnexin deficiency, however, affects neuronal development and function. Calreticulin-deficient and transgenic mice have revealed that calreticulin and the endoplasmic reticulum may be upstream regulators in the Ca2+-dependent pathways that control cellular differentiation and/or organ development. ![]() Calreticulin, a major Ca2+ binding (storage) chaperone in the endoplasmic reticulum, is a key component of the calreticulin/calnexin cycle which is responsible for the folding of newly synthesized proteins and glycoproteins and for quality control pathways in the endoplasmic reticulum. Its unique luminal environment consists of Ca2+ binding chaperones, which are involved in protein folding, posttranslational modification, Ca2+ storage and release, and lipid synthesis and metabolism. The endoplasmic reticulum is an intracellular organelle involved in virtually every cellular function.
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