由微管相关蛋白介导的肌动蛋白丝-微管相互作用的证据。
Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins.
作者信息
Griffith L M, Pollard T D
出版信息
J Cell Biol. 1978 Sep;78(3):958-65. doi: 10.1083/jcb.78.3.958.
Abstract
We have used low shear viscometry and electron microscopy to study the interaction between pure actin filaments and microtubules. Mixtures of microtubules having microtubule-associated proteins (MAPs) with actin filament have very high viscosities compared with the viscosities of the separate components. MAPs themselves also cause a large increase in the viscosity of actin filaments. In contrast, mixtures of actin filaments with tubulin polymers lacking MAPs have low viscosities, close to the sum of the viscosities of the separate components. Our interpretation of these observations is that there is an interaction between actin filaments and microtubules which requires MAPs. This interaction is inhibited by ATP and some related compounds. Electron micrographs of thin sections through mixtures of actin and microtubules show numerous close associations between the two polymers which may be responsible for their high viscosity.
摘要
我们利用低剪切粘度测定法和电子显微镜来研究纯肌动蛋白丝与微管之间的相互作用。与单独组分的粘度相比，含有微管相关蛋白（MAPs）的微管与肌动蛋白丝的混合物具有非常高的粘度。MAPs本身也会使肌动蛋白丝的粘度大幅增加。相比之下，肌动蛋白丝与缺乏MAPs的微管蛋白聚合物的混合物粘度较低，接近单独组分粘度之和。我们对这些观察结果的解释是，肌动蛋白丝与微管之间存在一种需要MAPs的相互作用。这种相互作用受到ATP和一些相关化合物的抑制。通过肌动蛋白和微管混合物的薄切片电子显微照片显示，这两种聚合物之间存在大量紧密结合，这可能是它们高粘度的原因。
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