轴突中的微管稳定性：一个古老谜题的新答案。
Microtubule stability in the axon: new answers to an old mystery.
机构信息
Drexel University College of Medicine, Philadelphia, PA 19129, USA.
出版信息
Neuron. 2013 Apr 10;78(1):3-5. doi: 10.1016/j.neuron.2013.03.012.
PMID:23583103
Abstract
It has been known for decades that a fraction of neuronal tubulin is insoluble in cold and also resistant to calcium as well as drugs that depolymerize microtubules. In this issue of Neuron, Song et al. (2013) suggest that this unusual stability results from the polyamination of tubulin by transglutaminase.
摘要
几十年来，人们已经知道，一小部分神经元微管蛋白在冷环境下不溶解，而且对钙以及会使微管解聚的药物有抗性。在本期的《神经元》杂志中，Song 等人（2013）提出，这种不寻常的稳定性是由转谷氨酰胺酶使微管蛋白多聚胺化引起的。
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