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Calreticulin: Challenges Posed By The Intrinsically Disordered Nature Of Calreticulin To The Study Of Its Function, Lilian Varricchio, Mario Falchi, Massimiliano Dall'ora, Benedittis, Caterina De Benedittis, Alessandra Ruggeri, Vladimir N. Uversky, Anna Rita Migliaccio

Molecular Medicine Faculty Publications

Calreticulin is a Ca²⁺-binding chaperone protein, which resides mainly in the endoplasmic reticulum but also found in other cellular compartments including the plasma membrane. In addition to Ca²⁺, calreticulin binds and regulates almost all proteins and most of the mRNAs deciding their intracellular fate. The potential functions of calreticulin are so numerous that identification of all of them is becoming a nightmare. Still the recent discovery that patients affected by the Philadelphia-negative myeloproliferative disorders essential thrombocytemia or primary myelofibrosis not harboring JAK2 mutations carry instead calreticulin mutations disrupting its C-terminal domain has highlighted the clinical need …