Kinesins are molecular motors that use energy derived from ATP turnover to walk along microtubules, or when at the microtubule end, regulate growth or shrinkage. All kinesins that regulate microtubule dynamics have long residence times at microtubule ends, whereas those that only walk have short end‐residence times. Here, we identify key amino acids involved in end binding by showing that when critical residues from Kinesin‐13, which depolymerises microtubules, are introduced into Kinesin‐1, a walking kinesin with no effect on microtubule dynamics, the end‐residence time is increased up to several‐fold. This indicates that the interface between the kinesin motor domain and the microtubule is malleable and can be tuned to favour either lattice or end binding.

中文翻译：

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鉴定调节驱动蛋白与微管末端相互作用的关键残基。

驱动蛋白是分子马达，其利用源自ATP转换的能量来沿着微管行走，或者当在微管末端时，调节生长或收缩。所有调节微管动力学的驱动蛋白在微管末端的停留时间均较长，而仅行走的那些驱动蛋白的末端停留时间较短。在这里，我们通过显示将解聚微管的Kinesin-13的关键残基引入Kinesin-1（一种对微管动力学无影响的步行型驱动蛋白），从而确定了末端结合中涉及的关键氨基酸。多达几倍。这表明驱动蛋白运动域和微管之间的界面是可延展的，可以进行调整以利于晶格或末端结合。