Tubulin polyglutamylation stimulates spastin-mediated microtubule severing

被引:200
|
作者
Lacroix, Benjamin [1 ,2 ]
van Dijk, Juliette [1 ,2 ]
Gold, Nicholas D. [1 ,2 ]
Guizetti, Julien [3 ]
Aldrian-Herrada, Gudrun [1 ,2 ]
Rogowski, Krzysztof [1 ,2 ]
Gerlich, Daniel W. [3 ]
Janke, Carsten [1 ,2 ,4 ,5 ,6 ]
机构
[1] Univ Montpellier 2, CRBM, CNRS, UMR 5237, F-34293 Montpellier, France
[2] Univ Montpellier I, CRBM, CNRS, UMR 5237, F-34293 Montpellier, France
[3] ETH, Swiss Fed Inst Technol, Inst Biochem, CH-8093 Zurich, Switzerland
[4] Inst Curie, F-91405 Orsay, France
[5] CNRS, UMR 3306, F-91405 Orsay, France
[6] INSERM, U1005, F-91405 Orsay, France
来源
JOURNAL OF CELL BIOLOGY | 2010年 / 189卷 / 06期
关键词
BETA-TUBULIN; ALPHA-TUBULIN; KATANIN; PROTEIN; POLYGLYCYLATION; GLUTAMYLATION; PROCESSIVITY; CYTOKINESIS; PARAPLEGIA; INTERACTS;
D O I
10.1083/jcb.201001024
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Posttranslational glutamylation of tubulin is present on selected subsets of microtubules in cells. Although the modification is expected to contribute to the spatial and temporal organization of the cytoskeleton, hardly anything is known about its functional relevance. Here we demonstrate that glutamylation, and in particular the generation of long glutamate side chains, promotes the severing of microtubules. In human cells, the generation of long side chains induces spastin-dependent microtubule disassembly and, consistently, only microtubules modified by long glutamate side chains are efficiently severed by spastin in vitro. Our study reveals a novel control mechanism for microtubule mass and stability, which is of fundamental importance to cellular physiology and might have implications for diseases related to microtubule severing.
引用
收藏
页码:945 / 954
页数:10
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