Pasdar M, Krzeminski K A, Nelson W J
Institute for Cancer Research, Philadelphia, Pennsylvania 19111.
J Cell Biol. 1991 May;113(3):645-55. doi: 10.1083/jcb.113.3.645.
Desmosomes are major components of the intercellular junctional complex in epithelia. They consist of at least eight different cytoplasmic and integral membrane proteins that are organized into two biochemically and structurally distinct domains: the cytoplasmic plaque and membrane core. We showed previously that in MDCK epithelial cells major components of the cytoplasmic plaque (desmoplakin I and II; DPI/II) and membrane core domains (desmoglein I; DGI) initially enter a pool of proteins that is soluble in buffers containing Triton X-100, and then titrate into an insoluble pool before their arrival at the plasma membrane (Pasdar, M., and W. J. Nelson. 1988. J. Cell Biol. 106:677-685; Pasdar. M., and W. J. Nelson. 1989. J. Cell Biol. 109:163-177). We have now examined whether either the soluble or insoluble pool of these proteins represents an intracellular site for assembly and interactions between the domains before their assembly into desmosomes at the plasma membrane. Interactions between the Triton X-100-soluble pools of DPI/II and DGI were analyzed by sedimentation of extracted proteins in sucrose gradients. Results show distinct differences in the sedimentation profiles of these proteins, suggesting that they are not associated in the Triton X-100-soluble pool of proteins; this was also supported by the observation that DGI and DPI/II could not be coimmunoprecipitated in a complex with each other from sucrose gradient fractions. Immunofluorescence analysis of the insoluble pools of DPI/II and DGI, in cells in which desmosome assembly had been synchronized, showed distinct differences in the spatial distributions of these proteins. Furthermore, DPI/II and DGI were found to be associated with different elements of cytoskeleton; DPI/II were located along cytokeratin intermediate filaments, whereas DGI appeared to be associated with microtubules. The regulatory role of cytoskeletal elements in the intracellular organization and assembly of the cytoplasmic plaque and membrane core domains, and their integration into desmosomes on the plasma membrane is discussed.
桥粒是上皮细胞间连接复合体的主要组成部分。它们由至少八种不同的细胞质和整合膜蛋白组成,这些蛋白被组织成两个在生化和结构上不同的结构域:细胞质斑和膜核心。我们之前表明,在MDCK上皮细胞中,细胞质斑的主要成分(桥粒斑蛋白I和II;DPI/II)和膜核心结构域(桥粒芯糖蛋白I;DGI)最初进入一个可溶于含有Triton X-100的缓冲液的蛋白质池,然后在它们到达质膜之前滴定到一个不溶性池中(帕斯达,M.,和W. J. 尼尔森。1988年。《细胞生物学杂志》106:677 - 685;帕斯达,M.,和W. J. 尼尔森。1989年。《细胞生物学杂志》109:163 - 177)。我们现在研究了这些蛋白质的可溶性或不溶性池是否代表了它们在质膜上组装成桥粒之前,各结构域之间进行组装和相互作用的细胞内位点。通过在蔗糖梯度中对提取的蛋白质进行沉降分析,研究了DPI/II和DGI的Triton X-100可溶性池之间的相互作用。结果显示这些蛋白质的沉降图谱有明显差异,表明它们在Triton X-100可溶性蛋白质池中不相关;从蔗糖梯度级分中不能将DGI和DPI/II相互共免疫沉淀的观察结果也支持了这一点。对桥粒组装已同步化的细胞中DPI/II和DGI的不溶性池进行免疫荧光分析,结果显示这些蛋白质的空间分布有明显差异。此外,发现DPI/II和DGI与细胞骨架的不同成分相关;DPI/II沿着细胞角蛋白中间丝定位,而DGI似乎与微管相关。讨论了细胞骨架成分在细胞质斑和膜核心结构域的细胞内组织和组装以及它们整合到质膜上的桥粒中的调节作用。