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.

中文翻译：

---

一条尾巴的故事：IGF-1R致癌力背后的秘密。

长期以来，人们一直认为胰岛素样生长因子1受体（IGF-1R）的C端尾部会驱动该受体的许多致癌作用。在本期《科学信号》中，Rieger等人。已有研究表明，IGF-1R的Tyr ¹²⁵⁰和Tyr ¹²⁵¹以细胞粘附依赖性方式被自身磷酸化，从而揭示了迁移细胞中IGF-1R以前未知的质膜-高尔基体运输途径，这是恶性表型的组成部分。