BINDING OF MYOSIN-I TO MEMBRANE-LIPIDS
BINDING OF MYOSIN-I TO MEMBRANE-LIPIDS
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DOI：
10.1038/340565a0
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发表时间：
1989-08-17
期刊：
影响因子：
64.8
通讯作者：
POLLARD, TD
中科院分区：
文献类型：
--
作者：
ADAMS, RJ;POLLARD, TD
被称为肌球蛋白-I的单头肌球蛋白首先从原生动物阿米巴中分离出来，随后在其他细胞中得到鉴定（参考文献2）。我们以前报道的证据表明，肌球蛋白-I是负责运动的膜，提取自阿米巴，沿着肌动蛋白的体外3。在这里，我们第一次表明，肌球蛋白-I可以直接绑定到NaOH提取的膜分离阿米巴和囊泡的纯脂质具有足够的亲和力广泛的结合在细胞中。膜结合肌球蛋白-I可能提供了许多细胞运动的机制，以前认为涉及丝状肌球蛋白-II。
THE single-headed myosins called myosin-I were first isolated from the protozoanAcanthamoeba1and subsequently identified in other cells (reviewed in ref. 2). We previously reported evidence that myosin-I is responsible for the movement of membranes, extracted fromAcanthamoeba, along actin filamentsin vitro3. Here we show for the first time that myosin-I can bind directly to NaOH-extracted membranes isolated fromAcanthamoebaand to vesicles of pure lipids with an affinity sufficient for extensive binding in the cell. Membrane-bound myosin-I may provide a mechanism for many cellular movements previously thought to involve filamentous myosin-II.