A Direct Interaction with NEDD1 Regulates γ-Tubulin Recruitment to the Centrosome

被引:39
|
作者
Manning, Jantina A. [1 ,2 ]
Shalini, Sonia [1 ]
Risk, Joanna M. [3 ]
Day, Catherine L. [3 ]
Kumar, Sharad [1 ,2 ]
机构
[1] SA Pathol, Ctr Canc Biol, Adelaide, SA, Australia
[2] Univ Adelaide, Dept Med, Adelaide, SA 5001, Australia
[3] Univ Otago, Dept Biochem, Dunedin, New Zealand
来源
PLOS ONE | 2010年 / 5卷 / 03期
基金
英国医学研究理事会;
关键词
MICROTUBULE NUCLEATION; RING COMPLEX; SPINDLE; PROTEIN; LOCALIZATION; CEP192;
D O I
10.1371/journal.pone.0009618
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The centrosome is the primary microtubule organizing centre of the cell. gamma-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of gamma-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat containing protein. Here we demonstrate that NEDD1 is likely to be oligomeric in vivo and binds directly to gamma-tubulin through a small region of just 62 residues at the carboxyl-terminus of the protein. This carboxyl-terminal domain that binds gamma-tubulin has a helical structure and is a stable tetramer in solution. Mutation of residues in NEDD1 that disrupt binding to gamma-tubulin result in a mis-localization of gamma-tubulin away from the centrosome. Hence, this study defines the binding site on NEDD1 that is required for its interaction with gamma-tubulin, and shows that this interaction is required for the correct localization of gamma-tubulin.
引用
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页数:12
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