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在微管末端移动。

Surfing on microtubule ends.

作者信息

Carvalho Pedro, Tirnauer Jennifer S, Pellman David

机构信息

Departments of Pediatric Oncology, Dana-Farber Cancer Institute and Pediatric Hematology/Oncology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.

出版信息

Trends Cell Biol. 2003 May;13(5):229-37. doi: 10.1016/s0962-8924(03)00074-6.

Abstract

A crowd of proteins seems to have gathered around the plus-ends of microtubules. A rapidly expanding group of proteins known as plus-end tracking proteins (+TIPs) have been identified that seem to be able to 'surf' the dynamic ends of microtubules. Microtubule plus-ends exist in multiple conformational and chemical states. In principle, altering this plus-end microenvironment is an appealing way for regulators such as the +TIPS to control microtubule dynamics; however, specific mechanisms are poorly defined. Here, we focus on new findings addressing the underlying mechanisms of plus-end tracking and the mechanisms by which +TIPS control microtubule dynamics. We review the evidence that plus-end-binding and the control of microtubule dynamics are mechanistically linked. We also consider the possibility that, by studying +TIPs, we might learn more about the dynamic structural changes at the microtubule ends that are at the heart of dynamic instability.

摘要

一群蛋白质似乎聚集在微管的正端周围。已鉴定出一组迅速扩大的被称为正端追踪蛋白(+TIPs)的蛋白质,它们似乎能够“冲浪”微管的动态末端。微管正端存在多种构象和化学状态。原则上,改变这种正端微环境是像+TIPs这样的调节因子控制微管动力学的一种有吸引力的方式;然而,具体机制尚不清楚。在这里,我们关注关于正端追踪潜在机制以及+TIPs控制微管动力学机制的新发现。我们回顾了正端结合与微管动力学控制在机制上相关的证据。我们还考虑了这样一种可能性,即通过研究+TIPs,我们可能更多地了解微管末端动态结构变化,而这些变化是动态不稳定性的核心。

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