title: Mutant calreticulin: when a chaperone becomes intrusive.
abstract: In this issue of Blood, Marty et al, Chachoua et al, and Araki et al report results of studies unraveling the molecular pathogenesis of CALR-mutant myeloproliferative neoplasms (MPNs). Together, these 3 reports define a novel disease paradigm, whereby a mutant chaperone constitutively activates receptor signaling through an abnormal interaction with the thrombopoietin (TPO) receptor (MPL).
authors.affiliation: FONDAZIONE ISTITUTO DI RICOVERO E CURA A CARATTERE SCIENTIFICO POLICLINICO SAN MATTEO; UNIVERSITY OF PAVIA.
authors.forename: Mario
authors.identifier: http://orcid.org/0000-0001-6984-8817
authors.initials: M
authors.lastname: Cazzola
mesh_terms: D000818:Animals; D037282:Calreticulin / Q000378:metabolism*; D019337:Hematologic Neoplasms / Q000378:metabolism*; D006801:Humans; D054643:INDEL Mutation; D060588:LIM Domain Proteins / Q000378:metabolism*; D008533:Megakaryocytes / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism*; D009154:Mutation; D009196:Myeloproliferative Disorders / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism*; D055728:Primary Myelofibrosis / Q000378:metabolism*; D053628:Receptors, Thrombopoietin / Q000378:metabolism*; D013922:Thrombocytosis / Q000378:metabolism*
chemical_list: D037282:Calreticulin; D060588:LIM Domain Proteins; D009124:Muscle Proteins; D009363:Neoplasm Proteins; D053628:Receptors, Thrombopoietin