波形蛋白与膜相互作用中的位点特异性：中间丝亚基通过其头部结构域与质膜结合。
Site specificity in vimentin-membrane interactions: intermediate filament subunits associate with the plasma membrane via their head domains.
作者信息
Georgatos S D, Weaver D C, Marchesi V T
出版信息
J Cell Biol. 1985 Jun;100(6):1962-7. doi: 10.1083/jcb.100.6.1962.
Abstract
Fragments of vimentin, generated by chemical or enzymatic cleavages, were analyzed for their capacity to bind to human inverted erythrocyte membrane vesicles. Only peptides comprising the amino-terminal head domain of vimentin molecules were competent in associating with the membranes. In vitro studies also demonstrated that isolated ankyrin (the major vimentin acceptor site on the membrane) binds to an oligomeric species of vimentin and prevents the formation of characteristic 10-nm filaments. These data, taken together with the observation that the NH2-terminal end of vimentin is implicated in the polymerization process (Traub, P., and C. Vorgias, J. Cell Sci., 1983, 63:43-67), imply that intermediate filaments may contact the membrane in an end-on fashion, using the exposed head domains of their terminal subunits.
摘要
对通过化学或酶切产生的波形蛋白片段进行分析，以检测它们与人类反转红细胞膜囊泡结合的能力。只有包含波形蛋白分子氨基末端头部结构域的肽才能与膜结合。体外研究还表明，分离出的锚蛋白（膜上波形蛋白的主要受体位点）与波形蛋白的寡聚体结合，并阻止特征性10纳米细丝的形成。这些数据，再加上波形蛋白的氨基末端参与聚合过程的观察结果（Traub, P.和C. Vorgias, 《细胞科学杂志》，1983年，63:43 - 67），表明中间丝可能以末端对接的方式与膜接触，利用其末端亚基暴露的头部结构域。
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