The contribution of αβ-tubulin curvature to microtubule dynamics

被引:156
作者
Brouhard, Gary J. [1 ]
Rice, Luke M. [2 ,3 ]
机构
[1] McGill Univ, Dept Biol, Montreal, PQ H3A 1B1, Canada
[2] Univ Texas SW Med Ctr Dallas, Dept Biophys, Dallas, TX 75390 USA
[3] Univ Texas SW Med Ctr Dallas, Dept Biochem, Dallas, TX 75390 USA
基金
加拿大自然科学与工程研究理事会; 美国国家科学基金会; 美国国家卫生研究院; 加拿大健康研究院;
关键词
PLUS-END-TRACKING; KINESIN-RELATED PROTEIN; CENTROMERE-ASSOCIATED KINESIN; SELF-ASSEMBLY KINETICS; YEAST MITOTIC SPINDLE; STATHMIN-LIKE DOMAIN; STRUCTURAL BASIS; NDC80; COMPLEX; IN-VITRO; DOUBLECORTIN RECOGNIZES;
D O I
10.1083/jcb.201407095
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Microtubules are dynamic polymers of alpha beta-tubulin that form diverse cellular structures, such as the mitotic spindle for cell division, the backbone of neurons, and axonemes. To control the architecture of microtubule networks, microtubule-associated proteins (MAPs) and motor proteins regulate microtubule growth, shrinkage, and the transitions between these states. Recent evidence shows that many MAPs exert their effects by selectively binding to distinct conformations of polymerized or unpolymerized alpha beta-tubulin. The ability of alpha beta-tubulin to adopt distinct conformations contributes to the intrinsic polymerization dynamics of microtubules. alpha beta-Tubulin conformation is a fundamental property that MAPs monitor and control to build proper microtubule networks.
引用
收藏
页码:323 / 334
页数:12
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