Actin-membrane interaction in fibroblasts: what proteins are involved in this association?
Actin-membrane interaction in fibroblasts: what proteins are involved in this association?
复制标题
成纤维细胞中肌动蛋白-膜相互作用：哪些蛋白质参与这种关联？
DOI：
10.1083/jcb.99.1.95s
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Burridge,K
中科院分区：
文献类型：
--
作者：
Mangeat,P;Burridge,K
在这篇综述中，我们讨论了一些蛋白质的作用，在连接肌动蛋白的成纤维细胞质膜已被建议。我们专注于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具有与红细胞血影蛋白相似的肌动蛋白膜附着的组织和功能。我们在活的成纤维细胞中沉淀出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组织和功能上的相似性提出了质疑。成纤维细胞血影蛋白的细胞内沉淀不影响主要的肌动蛋白含结构的完整性，应力纤维微丝束。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细胞中检查的中间丝的波形蛋白类的冷凝和改变的分布。虽然成纤维细胞血影蛋白可能在某些皮质、膜下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是如此之小。已经发现几种蛋白质集中在应力纤维的末端，肌动蛋白丝终止于焦点接触处。这些蛋白质中的两种，α-辅肌动蛋白和fimalin，具有表明它们不参与纤维束末端与膜的附着的性质，但更可能参与纤维束内细丝的组织和交联。另一方面，黏着斑蛋白和talin是两种相互作用的蛋白质，并且可以形成微丝束末端与焦点接触膜之间的连接链的一部分。然而，它们在这种连接中的作用尚未确定，需要进一步的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组分，特别是在质膜中。
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.