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锚蛋白B在晶状体结构和生物力学中的作用:不仅是连接,还有更多。

Ankyrin-B in lens architecture and biomechanics: Just not tethering but more.

作者信息

Rao Ponugoti Vasantha, Maddala Rupalatha

机构信息

a Department of Ophthalmology , Duke University School of Medicine , Durham , NC , USA.

b Department of Pharmacology & Cancer Biology , Duke University School of Medicine , Durham , NC , USA.

出版信息

Bioarchitecture. 2016;6(2):39-45. doi: 10.1080/19490992.2016.1156284.

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.

摘要

锚蛋白是一类特征明确的后生动物衔接蛋白,在将各种跨膜蛋白连接到其下方的血影蛋白 - 肌动蛋白细胞骨架中起关键作用;然而,对其在组织结构和力学中的作用机制仍不清楚。在此,我们对最近一项研究进行评论,该研究表明锚蛋白B通过调节外周蛋白、肌营养不良蛋白/肌营养不良聚糖、神经细胞黏附分子(NrCAM)以及血影蛋白 - 肌动蛋白网络蛋白的膜组织,在维持晶状体纤维细胞的六边形形状和径向排列方面发挥关键作用,并揭示锚蛋白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通过参与膜锚定和血影蛋白 - 肌动蛋白骨架、支架蛋白和细胞黏附蛋白组织所需的关键蛋白 - 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。

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