DLG与KIF13B之间相互作用揭示的MAGUK家族蛋白GK结构域识别目标蛋白的非经典模式  

An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B

作　　者：朱金伟 Yuan Shang Yitian Xia Rongguang Zhang Mingjie Zhang 

机构地区：[1]中国科学院上海生命科学研究院生物化学与细胞生物学研究所 [2]不详

出　　处：《科学新闻》2017年第4期184-184,共1页Science News

基　　金：国家自然科学基金、科技部、香港研究资助局的支持

摘　　要：MAGUK家族蛋白都含有一个特征的GK结构域。MAGUK家族蛋白在控制细胞极性和调控神经信号传导过程中发挥着不可或缺的作用。目前，MAGUK-GK结构域已知的识别目标蛋白的模式是结合一段磷酸化的短肽。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.

关 键 词：蛋白 经典模式 结构 家族 相互作用 识别 传导过程 

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