Steinböck F A, Wiche G
Institute of Biochemistry and Molecular Cell Biology, University of Vienna, Vienna Biocenter, Austria.
Biol Chem. 1999 Feb;380(2):151-8. doi: 10.1515/BC.1999.023.
Plectin is a cytoskeletal protein of >500 kDa that forms dumbbell-shaped homodimers comprising a central parallel alpha-helical coiled coil rod domain flanked by globular domains, thus providing a molecular backbone ideally suited to mediate the protein's interactions with an array of other cytoskeletal elements. Plectin self-associates and interacts with actin and intermediate filament cytoskeleton networks at opposite ends, and it binds at both ends to the hemidesmosomal transmembrane protein integrin beta-4, and likely to other junctional proteins. The central coiled coil rod domain can form bridges over long stretches and serves as a flexible linker between the structurally diverse N-terminal domain and the highly conserved C-terminal domain. Plectin is also a target of p34cdc2 kinase that regulates its dissociation from intermediate filaments during mitosis.
网蛋白是一种分子量超过500 kDa的细胞骨架蛋白，它形成哑铃状同源二聚体，由一个中央平行α-螺旋卷曲螺旋杆状结构域和两侧的球状结构域组成，从而提供了一个理想的分子骨架，适合介导该蛋白与一系列其他细胞骨架成分的相互作用。网蛋白在两端与肌动蛋白和中间丝细胞骨架网络发生自缔合和相互作用，并且它在两端与半桥粒跨膜蛋白整合素β-4结合，也可能与其他连接蛋白结合。中央卷曲螺旋杆状结构域可以在很长的距离上形成桥梁，并作为结构多样的N端结构域和高度保守的C端结构域之间的柔性连接体。网蛋白也是p34cdc2激酶的作用靶点，该激酶在有丝分裂期间调节其与中间丝的解离。
