Goldman A E, Maul G, Steinert P M, Yang H Y, Goldman R D
Proc Natl Acad Sci U S A. 1986 Jun;83(11):3839-43. doi: 10.1073/pnas.83.11.3839.
Four proteins of Mr approximately equal to 60,000, 65,000, 67,000, and 70,000 coisolate with the major intermediate filament (IF) structural proteins of BHK-21 cells. These proteins are keratin-like, they form distinctive paracrystals in vitro, and they are concentrated at the nuclear surface. Since these properties indicate similarities with the nuclear lamins, we have prepared conventional fractions of BHK-21 nuclei from which the same type of paracrystal is obtained. Furthermore, biochemical and immunological data demonstrate that the lamins are identical to the Mr 60,000-70,000 proteins found in IF preparations, and both sets of proteins are similar to keratin. These results suggest that an IF-like protein network is present in the nuclear lamina. We speculate that in some unknown way this network connects to the cytoplasmic IF network that courses from the juxtanuclear region to the cell surface. These proposed interconnecting networks may form part of the infrastructure of cytoskeletal-nuclear matrix-connecting links involved in signal transmission between the nuclear and cytoplasmic compartments of eukaryotic cells.
四种分子量约为60,000、65,000、67,000和70,000的蛋白质与BHK - 21细胞的主要中间丝（IF）结构蛋白共分离。这些蛋白质类似角蛋白，在体外形成独特的副晶体，并且集中在核表面。由于这些特性表明它们与核纤层蛋白相似，我们制备了BHK - 21细胞核的常规组分，从中获得了相同类型的副晶体。此外，生化和免疫学数据表明，核纤层蛋白与在中间丝制剂中发现的分子量为60,000 - 70,000的蛋白质相同，并且这两组蛋白质都与角蛋白相似。这些结果表明核纤层中存在类似中间丝的蛋白质网络。我们推测，以某种未知方式，这个网络与从核周区域延伸到细胞表面的细胞质中间丝网络相连。这些提议的相互连接的网络可能构成参与真核细胞细胞核与细胞质区室之间信号传递的细胞骨架 - 核基质连接基础设施的一部分。
