Structural basis of EB1 effects on microtubule dynamics

被引:22
|
作者
Coquelle, Frederic M. [1 ]
Vitre, Benjamin [1 ]
Arnal, Isabelle [1 ]
机构
[1] Univ Rennes 1, Inst Fed Rech 140, CNRS, UMR 6026, F-35042 Rennes, France
关键词
dynamic instability; end-binding 1 (EB1); microtubule-associated protein (MAP); plus end tracking protein ( plus TIP); tubulin sheet; PLUS-END-TRACKING; SLOWLY HYDROLYZABLE ANALOG; SURFACE LATTICE; CRYOELECTRON MICROSCOPY; INTERPHASE MICROTUBULES; ELECTRON TOMOGRAPHY; GTP HYDROLYSIS; IN-VITRO; TUBULIN; POLYMERIZATION;
D O I
10.1042/BST0370997
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
+TIPs (plus-end tracking proteins) are an increasing group of molecules that localize preferentially to the end of growing microtubules. +TIPs regulate microtubule dynamics and contribute to the organization of the microtubular network within the cell. Thus they participate in a wide range of cellular processes including cell division, motility and morphogenesis. EB1 (end-binding 1) is a highly conserved key member of the +TIP group that has been shown to modulate microtubule dynamics both in vitro and in cells. EB1 is involved in accurate chromosome segregation during mitosis and in the polarization of the microtubule cytoskeleton in migrating cells. Here, we review recent in vitro studies that have started to reveal a regulating activity of EB1, and its yeast orthologue Mal3p, on microtubule structure. In particular, we examine how EB1-mediated changes in the microtubule architecture may explain its effects on microtubule dynamics.
引用
收藏
页码:997 / 1001
页数:5
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