Center of Research in Myology, Institute of Myology, UMRS 974, INSERM, Sorbonne Université, F-75013 Paris, France.
Department of Physiology, Pitié-Salpêtrière Hospital, Sorbonne Université, F-75013 Paris, France.
Mol Biol Cell. 2019 Mar 1;30(5):579-590. doi: 10.1091/mbc.E18-11-0718. Epub 2019 Jan 2.
Clathrin plaques are stable features of the plasma membrane observed in several cell types. They are abundant in muscle, where they localize at costameres that link the contractile apparatus to the sarcolemma and connect the sarcolemma to the basal lamina. Here, we show that clathrin plaques and surrounding branched actin filaments form microdomains that anchor a three-dimensional desmin intermediate filament (IF) web. Depletion of clathrin plaque and branched actin components causes accumulation of desmin tangles in the cytoplasm. We show that dynamin 2, whose mutations cause centronuclear myopathy (CNM), regulates both clathrin plaques and surrounding branched actin filaments, while CNM-causing mutations lead to desmin disorganization in a CNM mouse model and patient biopsies. Our results suggest a novel paradigm in cell biology, wherein clathrin plaques act as platforms capable of recruiting branched cortical actin, which in turn anchors IFs, both essential for striated muscle formation and function.
网格蛋白斑是几种细胞类型中观察到的稳定的质膜特征。它们在肌肉中含量丰富,在肌肉中,它们定位于连接收缩装置与肌膜并将肌膜连接到基膜的肌节上。在这里,我们表明网格蛋白斑和周围分支的肌动蛋白丝形成微域,锚定三维结蛋白中间丝(IF)网。网格蛋白斑和分支肌动蛋白成分的耗竭导致细胞质中结蛋白缠结的积累。我们表明,导致核纤层肌病(CNM)的动力蛋白 2 调节网格蛋白斑和周围分支的肌动蛋白丝,而导致 CNM 的突变导致 CNM 小鼠模型和患者活检中的结蛋白解聚。我们的结果表明了细胞生物学中的一个新范例,其中网格蛋白斑作为能够招募分支皮质肌动蛋白的平台,而分支皮质肌动蛋白反过来又锚定 IF,这对于横纹肌的形成和功能都是必不可少的。