Vallee R B, Wall J S, Paschal B M, Shpetner H S
Cell Biology Group, Worcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545.
Nature. 1988 Apr 7;332(6164):561-3. doi: 10.1038/332561a0.
Dynein, an ATPase, is the force-generating protein in cilia and flagella. It has long been speculated that cytoplasmic microtubules contain a related enzyme involved in cell division or in intracellular organelle transport. A 'cytoplasmic dynein' has been described in sea urchin eggs, but because the egg stockpiles precursors for both cytoplasmic and ciliary microtubules, the role of this enzyme in the cell has remained unresolved. We recently found that the microtubule-associated protein (MAP) 1C (ref. 6) from brain is a microtubule-activated ATPase that produces force in the direction corresponding to retrograde organelle transport in the cell. MAP 1C has several similar properties to ciliary and flagellar dynein. Here we show directly, using scanning transmission electron microscopy, that MAP 1C is structurally equivalent to the ciliary and flagellar enzyme and is the long-sought cytoplasmic analogue of this enzyme.
动力蛋白是一种ATP酶,是纤毛和鞭毛中产生动力的蛋白质。长期以来,人们一直推测细胞质微管中含有一种与细胞分裂或细胞内细胞器运输有关的相关酶。在海胆卵中已描述了一种“细胞质动力蛋白”,但由于卵中储存了细胞质微管和纤毛微管的前体,这种酶在细胞中的作用仍未明确。我们最近发现,来自大脑的微管相关蛋白(MAP)1C(参考文献6)是一种微管激活的ATP酶,它在与细胞中细胞器逆行运输相对应的方向上产生动力。MAP 1C与纤毛和鞭毛动力蛋白有几个相似的特性。在这里,我们使用扫描透射电子显微镜直接表明,MAP 1C在结构上等同于纤毛和鞭毛酶,并且是这种酶长期以来寻找的细胞质类似物。