Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity
Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity
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DOI：
10.1073/pnas.1207467109
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发表时间：
2012-09-25
影响因子：
11.1
通讯作者：
Jedd, Gregory
中科院分区：
文献类型：
--
作者：
Lai, Julian;Koh, Chuan Hock;Jedd, Gregory
像动物和植物一样，多细胞真菌拥有允许细胞间通讯和运输的细胞间通道（隔膜孔）。在这里，使用MS的Woronin体相关蛋白质和生物信息学方法，确定相关蛋白质的组合物和字符的基础上，我们确定了17个中隔孔相关（SPA）的蛋白质，定位到中隔孔环和孔为中心的焦点。SPA蛋白质在一级序列水平上不同源，但与内在无序的蛋白质共享整体物理性质。一些SPA蛋白在隔膜孔处形成聚集体，并且体外组装测定表明通过主要涉及α-螺旋和无序结构的非淀粉样机制聚集。SPA功能丧失表型包括过度分隔、中隔孔变性和不受控制的Woronin体激活。总之，我们的数据确定中隔孔作为一个复杂的亚细胞区室和焦点的非结构化蛋白质控制细胞间连接的各个方面的组装。
Like animals and plants, multicellular fungi possess cell-to-cell channels (septal pores) that allow intercellular communication and transport. Here, using a combination of MS of Woronin body-associated proteins and a bioinformatics approach that identifies related proteins based on composition and character, we identify 17 septal pore-associated (SPA) proteins that localize to the septal pore in rings and pore-centered foci. SPA proteins are not homologous at the primary sequence level but share overall physical properties with intrinsically disordered proteins. Some SPA proteins form aggregates at the septal pore, and in vitro assembly assays suggest aggregation through a nonamyloidal mechanism involving mainly a-helical and disordered structures. SPA loss-of-function phenotypes include excessive septation, septal pore degeneration, and uncontrolled Woronin body activation. Together, our data identify the septal pore as a complex subcellular compartment and focal point for the assembly of unstructured proteins controlling diverse aspects of intercellular connectivity.