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The WW domain: Linking cell signalling to the membrane cytoskeleton [Review]

机译:WW域:将细胞信号传导与膜细胞骨架联系在一起[综述]

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摘要

The WW domain is one of the smallest yet most versatile protein-protein interaction modules. The ability of this simple domain to interact with a number of proline-containing ligands has resulted in a great deal of functional diversity. Most recently it has been shown that WW domain interactions can also be differentially regulated by tyrosine phosphorylation. Here we briefly review WW domain ligands and structure in comparison to SH3 domain ligands and structure and discuss recent findings with regard to the regulation of WW domain interactions by phosphorylation. In particular we describe the potential for differential binding of the b-dystroglycan WW domain ligand by dystrophin or caveolin-3 in skeletal muscle and show how this could act as a switch to alter the relative affinity of the muscle dystroglycan complex for caveolin-3 or dystrophin and utrophin. (C) 2002 Elsevier Science Inc. All rights reserved. [References: 42]
机译:WW结构域是最小但功能最多的蛋白质-蛋白质相互作用模块之一。该简单结构域与许多含脯氨酸的配体相互作用的能力导致了大量的功能多样性。最近已显示,酪氨酸磷酸化也可以差异地调节WW结构域的相互作用。在这里,我们简要回顾WW域配体和结构与SH3域配体和结构的比较,并讨论有关通过磷酸化调节WW域相互作用的最新发现。特别是,我们描述了骨骼肌中的抗肌萎缩蛋白或小窝蛋白3对b-dystroglycan WW域配体的差异结合的潜力,并显示了它如何作为改变肌营养不良聚糖复合物对小窝蛋白3或caveolin-3的相对亲和力的开关。肌营养不良蛋白和促肾上腺皮质激素。 (C)2002 Elsevier Science Inc.保留所有权利。 [参考:42]

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