Albrecht Douglas E, Froehner Stanley C
Department of Physiology and Biophysics, University of Washington, Seattle, 98195, USA.
Neurosignals. 2002 May-Jun;11(3):123-9. doi: 10.1159/000065053.
Dystrophin and its associated proteins were originally identified in skeletal muscle, where the complex provides mechanical stabilization to the sarcolemma during contraction. However, the dystrophin complex is also present at membrane specializations in many non-muscle cells, including synaptic sites in neurons. The function of the dystrophin complex at these sites is still unknown, but emerging results suggest that the dystrophin complex can function as a scaffold for signaling proteins. In this review, we examine the growing body of evidence that suggests the dystrophin complex may have a dual function: membrane stabilization and transmembrane signaling. We focus on the role of two dystrophin-associated proteins, syntrophin and dystrobrevin, in the formation of a signaling scaffold and review evidence suggesting a role in synapse formation and maintenance.
肌营养不良蛋白及其相关蛋白最初是在骨骼肌中被发现的，在收缩过程中，该复合物为肌膜提供机械稳定性。然而，肌营养不良蛋白复合物也存在于许多非肌肉细胞的膜特化部位，包括神经元的突触位点。肌营养不良蛋白复合物在这些位点的功能仍然未知，但新出现的结果表明，肌营养不良蛋白复合物可以作为信号蛋白的支架。在这篇综述中，我们研究了越来越多的证据，这些证据表明肌营养不良蛋白复合物可能具有双重功能：膜稳定和跨膜信号传导。我们重点关注两种与肌营养不良蛋白相关的蛋白，肌养蛋白和肌萎缩蛋白在信号支架形成中的作用，并综述表明其在突触形成和维持中起作用的证据。
