RET Functions as a Dual-Specificity Kinase that Requires Allosteric Inputs from Juxtamembrane Elements

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• 作者：Ivá ; n Plaza-Menacho¹ ; ⁷ ; ⁸ ; ^{ivan.plazamenacho@unibas.ch} ; Karin Barnouin² ; Rachael Barry⁵ ; Annabel Borg³ ; Mariam Orme⁵ ; Rakhee Chauhan¹ ; Stephane Mouilleron⁴ ; Rubé ; n J. Martí ; nez-Torres¹ ; Pascal Meier⁵ ; Neil Q. McDonald¹ ; ⁶ ; ^{neil.mcdonald@crick.ac.uk}
• 关键词：receptor tyrosine kinase ; RTK ; structure-function ; phosphorylation ; dual-specificity ; signaling ; oncogene ; Drosophila
• 刊名：Cell Reports
• 出版年：2016
• 出版时间：20 December 2016
• 年：2016
• 卷：17
• 期：12
• 页码：3319-3332
• 全文大小：4854 K
• 卷排序：17

文摘

The JM segment enhances RET catalytic domain activity Structural visualization of activation-loop phospho-S909 engaging the HRD motif Phospho-S909 arises from an intrinsic RET dual-specificity kinase activity RET αC hydrophobic pocket is a potential drug-targetable allosteric site