Institutional Repository, Institute of Psychology, Chinese Academy of Sciences
The proline-rich domain of tau plays a role in interactions with actin | |
H. J. He; X. S. Wang; R. Pan; D. L. Wang; M. N. Liu; R. Q. He | |
摘要 | Background: The microtubule-associated protein tau is able to interact with actin and serves as a cross-linker between the microtubule and actin networks. The microtubule-binding domain of tau is known to be involved in its interaction with actin. Here, we address the question of whether the other domains of tau also interact with actin. Results: Several tau truncation and deletion mutants were constructed, namely N-terminal region (tauN), proline-rich domain (tauPRD), microtubule binding domain (tauMTBD) and C-terminal region (tauC) truncation mutants, and microtubule binding domain (tauΔMTBD) and proline-rich domain/microtubule binding domain (tauΔPRD&MTBD) deletion mutants. The proline-rich domain truncation mutant (tauPRD) and the microtubule binding domain deletion mutant (tauΔMTBD) promoted the formation of actin filaments. However, actin assembly was not observed in the presence of the N-terminal and C-terminal truncation mutants. These results indicate that the proline-rich domain is involved in the association of tau with G-actin. Furthermore, results from co-sedimentation, solid phase assays and electron microscopy showed that the proline-rich domain is also capable of binding to F-actin and inducing F-actin bundles. Using solid phase assays to analyze apparent dissociation constants for the binding of tau and its mutants to F-actin resulted in a sequence of affinity for F-actin: tau >> microtubule binding domain > proline-rich domain. Moreover, we observed that the proline-rich domain was able to associate with and bundle F-actin at physiological ionic strength. Conclusion: The proline-rich domain is a functional structure playing a role in the association of tau with actin. This suggests that the proline-rich domain and the microtubule-binding domain of tau are both involved in binding to and bundling F-actin. |
关键词 | microtubule-associated proteins dynamic instability bundle formation in-vitro f-actin binding filaments tubulin organization spolymerization |
学科领域 | 分子生物学 |
2009 | |
语种 | 英语 |
发表期刊 | Bmc Cell Biology |
ISSN | 1471-2121 |
卷号 | 10 |
WOS记录号 | BMC:10.1186/1471-2121-10-81 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.psych.ac.cn/handle/311026/5783 |
专题 | 中国科学院心理研究所回溯数据库(1956-2010) |
通讯作者 | R. Q. He |
推荐引用方式 GB/T 7714 | H. J. He,X. S. Wang,R. Pan,et al. The proline-rich domain of tau plays a role in interactions with actin[J]. Bmc Cell Biology,2009,10. |
APA | H. J. He,X. S. Wang,R. Pan,D. L. Wang,M. N. Liu,&R. Q. He.(2009).The proline-rich domain of tau plays a role in interactions with actin.Bmc Cell Biology,10. |
MLA | H. J. He,et al."The proline-rich domain of tau plays a role in interactions with actin".Bmc Cell Biology 10(2009). |
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