Abstract
Recently, somatic mutations in the gene of endoplasmic reticulum (ER) chaperone protein, calreticulin (CALR), were established as one of the molecular hallmark alterations of essential thrombocythemia (ET). In vitro studies indicated that CARL mutations induce ET phenotype by specific activation of the thrombopoetin receptor (TpoR) both due to the loss of the ER retention motif (KDEL) and generation of a positively charged and methionine-rich C terminal stretch, a highly potent glycan binding site important for the association of calreticulin with TpoR.
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