Hoschuetzky H, Aberle H, Kemler R
Max-Planck-Institut für Immunobiologie, Freiburg, Germany.
J Cell Biol. 1994 Dec;127(5):1375-80. doi: 10.1083/jcb.127.5.1375.
Catenins mediate the linkage of classical cadherins with actin microfilaments and are part of a higher order protein structure by which cadherins are connected to other cytoplasmic and transmembrane proteins. The ratio of actin-bound to free cadherin-catenin complex, which varies depending on the type and growth rate of cells, is thought to be altered by cellular signals, such as those associated with mitosis, polarization of cells and growth factors during development. EGF induces an immediate tyrosine phosphorylation of beta-catenin and gamma-catenin (plakoglobin). We show here an association of the EGF-receptor with the cadherin-catenin complex. Using recombinant proteins we demonstrate the interaction of EGF-receptor and beta-catenin in in vitro kinase assays. This interaction is mediated by the evolutionarily conserved central "core" region of beta-catenin. These results suggest that catenins represent an important link between EGF-induced signal transduction and cadherin function.
连环蛋白介导经典钙黏着蛋白与肌动蛋白微丝的连接,并且是一种更高级蛋白质结构的一部分,通过该结构钙黏着蛋白与其他细胞质和跨膜蛋白相连。与游离钙黏着蛋白 - 连环蛋白复合物结合的肌动蛋白的比例因细胞类型和生长速率而异,据认为会受到细胞信号的改变,例如那些与有丝分裂、细胞极化以及发育过程中的生长因子相关的信号。表皮生长因子(EGF)诱导β - 连环蛋白和γ - 连环蛋白(桥粒斑蛋白)立即发生酪氨酸磷酸化。我们在此展示了表皮生长因子受体与钙黏着蛋白 - 连环蛋白复合物的关联。使用重组蛋白,我们在体外激酶测定中证明了表皮生长因子受体与β - 连环蛋白的相互作用。这种相互作用由β - 连环蛋白进化上保守的中央“核心”区域介导。这些结果表明连环蛋白代表了表皮生长因子诱导的信号转导与钙黏着蛋白功能之间的重要联系。