镜头结构和生物力学中的锚蛋白b:不仅仅是系住,而是更多

P. Rao, R. Maddala
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引用次数: 6

摘要

锚定蛋白是一个具有良好特征的后生动物适应蛋白家族,在将各种跨膜蛋白连接到潜在的谱蛋白-肌动蛋白细胞骨架中起关键作用;然而,对它们在组织结构和力学中的作用的机械理解仍然难以捉摸。最近的一项研究表明,锚蛋白b在维持晶状体纤维细胞的六角形和径向排列中起关键作用,通过调节周轴蛋白、肌营养不良蛋白/糖营养不良蛋白、NrCAM和谱动蛋白网络蛋白的膜组织,并揭示了锚蛋白b缺乏会损害晶状体纤维细胞的形状和力学性能。这些观察结果表明,锚蛋白b通过参与膜锚定和组织谱蛋白-肌动蛋白骨架、支架蛋白和细胞粘附蛋白所需的关键蛋白相互作用,在维持组织细胞结构、细胞形状和生物力学特性方面发挥重要作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Ankyrin-B in lens architecture and biomechanics: Just not tethering but more
ABSTRACT The ankyrins are a family of well-characterized metazoan adaptor proteins that play a key role in linking various membrane-spanning proteins to the underlying spectrin-actin cytoskeleton; a mechanistic understanding of their role in tissue architecture and mechanics, however, remains elusive. Here we comment on a recent study demonstrating a key role for ankyrin-B in maintaining the hexagonal shape and radial alignment of ocular lens fiber cells by regulating the membrane organization of periaxin, dystrophins/dystroglycan, NrCAM and spectrin-actin network of proteins, and revealing that ankyrin-B deficiency impairs fiber cell shape and mechanical properties of the ocular lens. These observations indicate that ankyrin-B plays an important role in maintaining tissue cytoarchitecture, cell shape and biomechanical properties via engaging in key protein: protein interactions required for membrane anchoring and organization of the spectrin-actin skeleton, scaffolding proteins and cell adhesive proteins.
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