Liem Ronald K H
Department of Pathology and Cell Biology, Columbia University Medical Center, New York, New York 10032.
Cold Spring Harb Perspect Biol. 2016 Oct 3;8(10):a018259. doi: 10.1101/cshperspect.a018259.
This review discusses the spectrin superfamily of proteins that function to connect cytoskeletal elements to each other, the cell membrane, and the nucleus. The signature domain is the spectrin repeat, a 106-122-amino-acid segment comprising three α-helices. α-actinin is considered to be the ancestral protein and functions to cross-link actin filaments. It then evolved to generate spectrin and dystrophin that function to link the actin cytoskeleton to the cell membrane, as well as the spectraplakins and plakins that link cytoskeletal elements to each other and to junctional complexes. A final class comprises the nesprins, which are able to bind to the nuclear membrane. This review discusses the domain organization of the various spectrin family members, their roles in protein-protein interactions, and their roles in disease, as determined from mutations, and it also describes the functional roles of the family members as determined from null phenotypes.
本综述讨论了血影蛋白超家族蛋白质，这些蛋白质的功能是将细胞骨架成分相互连接、连接细胞膜和细胞核。其标志性结构域是血影蛋白重复序列，这是一个由106 - 122个氨基酸组成的片段，包含三个α螺旋。α - 辅肌动蛋白被认为是原始蛋白，其功能是交联肌动蛋白丝。然后它进化产生了血影蛋白和肌营养不良蛋白，它们的功能是将肌动蛋白细胞骨架连接到细胞膜，还有光谱斑蛋白和斑蛋白，它们将细胞骨架成分相互连接并连接到连接复合体。最后一类包括核膜联蛋白，它们能够结合核膜。本综述讨论了各种血影蛋白家族成员的结构域组织、它们在蛋白质 - 蛋白质相互作用中的作用以及它们在疾病中的作用（由突变确定），还描述了从基因敲除表型确定的家族成员的功能作用。
