Cupers P, Jadhav A P, Kirchhausen T
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
J Biol Chem. 1998 Jan 23;273(4):1847-50. doi: 10.1074/jbc.273.4.1847.
Eps15 is a phosphorylation substrate of the epidermal growth factor receptor kinase. In vivo, it is largely found in complex with AP-2, the plasma membrane clathrin adaptor protein complex. Although AP-2 is uniformly distributed across the surface of clathrin-coated pits and vesicles, Eps15 is preferentially found in the rims of endocytic clathrin-coated pits (1). This observation suggests that Eps15 may disengage from AP-2 during coat formation. Here we use two new anti-Eps15 antibodies to show that, contrary to our own earlier suggestion, coated vesicles isolated from brain do not contain detectable amounts of Eps15. Furthermore, when AP-2 complexes that are saturated with Eps15 are used for in vitro assembly of clathrin-AP-2 coats, normal structures are formed that contain the expected amounts of clathrin and AP-2, but the amount of Eps15 present is dramatically lower than that of AP-2. We propose that during coated pit formation, addition of clathrin to the growing edge at the rim of the pit releases Eps15 from AP-2.
Eps15是表皮生长因子受体激酶的磷酸化底物。在体内,它主要与AP-2(质膜网格蛋白衔接蛋白复合体)形成复合物。尽管AP-2均匀分布在网格蛋白包被小窝和小泡的表面,但Eps15优先存在于内吞性网格蛋白包被小窝的边缘(1)。这一观察结果表明,Eps15可能在包被形成过程中与AP-2分离。在这里,我们使用两种新的抗Eps15抗体来表明,与我们自己早期的推测相反,从脑中分离的包被小泡不含可检测量的Eps15。此外,当用饱和了Eps15的AP-2复合物进行网格蛋白-AP-2包被的体外组装时,会形成正常结构,其中含有预期量的网格蛋白和AP-2,但存在的Eps15量显著低于AP-2。我们提出,在包被小窝形成过程中,在小窝边缘生长边缘添加网格蛋白会使Eps15从AP-2中释放出来。