An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B
An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B
复制标题
DLG 与 KIF13B 交互揭示的非典型 MAGUK GK 目标识别模式
DOI：
10.1016/j.str.2016.08.008
复制
发表时间：
2016-11-01
期刊：
影响因子：
5.7
通讯作者：
Zhang, Mingjie
中科院分区：
文献类型：
--
作者：
Zhu, Jinwei;Shang, Yuan;Zhang, Mingjie
The membrane-associated guanylate kinase (MAGUK) scaffold proteins share a signature guanylate kinase (GK) domain. Despite their diverse functional roles in cell polarity control and synaptic signaling, the currently known mode of action of MAGUK GK is via its binding to phosphorylated short peptides from target proteins. Here, we discover that the GK domain of DLG MAGUK binds to an unphosphorylated and autonomously folded domain within the stalk region (MAGUK binding stalk [MBS] domain) of a kinesin motor KIF13B with high specificity and affinity. The structure of DLG4 GK in complex with KIF13B MBS reveals the molecular mechanism governing this atypical GK/target recognition mode and provides insights into DLG/KIF13B complex-mediated regulation of diverse cellular processes such as asymmetric cell division. We further show that binding to non-phosphorylated targets is another general property of MAGUK GKs, thus expanding the mechanisms of action of the MAGUK family proteins.
