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Characterization of RET oncogenic activation in MEN2 inherited cancer syndromes. (A) MEN 2A RET mutation leaves an unpaired cysteine residue in a RET monomer to form an aberrant intermolecular disulfide bond with another mutated monomer. The two mutated RET molecules are constitutively dimerized and activated; (B) MEN 2B RET mutation activates tyrosines in the kinase domain and alters its substrate specificity leading to aberrant phosphorylation of substrates of RET receptor.
