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Abstract
The C-terminal tail of insulin-like growth factor 1 receptor (IGF-1R) has long been appreciated to drive much of this receptor’s oncogenic power. In this issue of Science Signaling, Rieger et al. have shown that Tyr1250 and Tyr1251 of IGF-1R are autophosphorylated in a cell adhesion–dependent manner, uncovering a previously unknown plasma membrane–Golgi trafficking route for IGF-1R in migratory cells, an integral part of the malignant phenotype.
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