Mangeat P, Burridge K
J Cell Biol. 1984 Jul;99(1 Pt 2):95s-103s. doi: 10.1083/jcb.99.1.95s.
In this review we discuss some of the proteins for which a role in linking actin to the fibroblast plasma membrane has been suggested. We focus on the family of proteins related to erythrocyte spectrin, proteins that have generally been viewed as having an organization and a function in actin-membrane attachment similar to those of erythrocyte spectrin. Experiments in which we precipitated the nonerythrocyte spectrin within living fibroblasts have led us to question this supposed similarity of organization and function of the nonerythrocyte and erythrocyte spectrins. Intracellular precipitation of fibroblast spectrin does not affect the integrity of the major actin-containing structures, the stress fiber microfilament bundles. Unexpectedly, however, we found that the precipitation of spectrin results in a condensation and altered distribution of the vimentin class of intermediate filaments in most cells examined. Although fibroblast spectrin may have a role in the attachment of some of the cortical, submembranous actin, it is surprising how little the intracellular immunoprecipitation of the spectrin affects the cells. Several proteins have been found concentrated at the ends of stress fibers, where the actin filaments terminate at focal contacts. Two of these proteins, alpha-actinin and fimbrin, have properties that suggest that they are not involved in the attachment of the ends of the bundles to the membrane but are more probably involved in the organization and cross-linking of the filaments within the bundles. On the other hand, vinculin and talin are two proteins that interact with each other and may form part of a chain of attachments between the ends of the microfilament bundles and the focal contact membrane. Their role in this attachment, however, has not been established and further work is needed to examine their interaction with actin and to identify any other components with which they may interact, particularly in the plasma membrane.
在本综述中，我们讨论了一些被认为在将肌动蛋白连接到成纤维细胞质膜中起作用的蛋白质。我们关注与红细胞血影蛋白相关的蛋白质家族，这些蛋白质通常被认为在肌动蛋白与膜的附着中具有与红细胞血影蛋白相似的结构和功能。我们在活的成纤维细胞中沉淀非红细胞血影蛋白的实验，使我们对非红细胞血影蛋白和红细胞血影蛋白在结构和功能上的这种假定相似性产生了质疑。成纤维细胞血影蛋白的细胞内沉淀并不影响主要含肌动蛋白结构（应力纤维微丝束）的完整性。然而，出乎意料的是，我们发现血影蛋白的沉淀导致在大多数被检测细胞中波形蛋白类中间丝发生凝聚并改变了分布。尽管成纤维细胞血影蛋白可能在一些皮质下膜性肌动蛋白的附着中起作用，但令人惊讶的是，血影蛋白的细胞内免疫沉淀对细胞的影响如此之小。已发现几种蛋白质集中在应力纤维的末端，肌动蛋白丝在粘着斑处终止于此。其中两种蛋白质，α - 辅肌动蛋白和丝束蛋白，其特性表明它们不参与束末端与膜的附着，而更可能参与束内丝的组织和交联。另一方面，纽蛋白和踝蛋白是两种相互作用的蛋白质，可能构成微丝束末端与粘着斑膜之间附着链的一部分。然而，它们在这种附着中的作用尚未确定，需要进一步开展工作来研究它们与肌动蛋白的相互作用，并确定它们可能相互作用的任何其他成分，特别是在质膜中。
