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Also known as: MPLV; TPOR; C-MPL; CD110; THPOR; THCYT2
In 1990, an oncogene, v-mpl, was identified from a mouse myeloproliferative leukemia virus capable of immortalizing myeloid hematopoietic cells from different lineages. In 1992, the human homologous gene c-mpl was cloned. Sequence data revealed that c-mpl encodes a protein homologous to members of the hematopoietic receptor superfamily. The presence of c-mpl antisense oligodeoxynucleotides inhibits megakaryocyte colony formation. The ligand for c-mpl, thrombopoietin, was cloned in 1994. Thrombopoietin is a master regulator of megakaryocytopoiesis and platelet formation. The protein CD110 encoded by the c-mpl gene is a 635 amino acid transmembrane domain with two extracellular cytokine receptor domains and two intracellular cytokine receptor box motifs. TPO-R-deficient mice are severely thrombocytopenic, emphasizing the essential role of CD110 and thrombopoietin in megakaryocyte and platelet formation. After binding to thrombopoietin, CD110 is dimerized, and the JAK family of non-receptor tyrosine kinases, as well as the STAT family, MAPK family, adapter protein Shc, and the receptor itself are tyrosine-phosphorylated.