Xiubo Du
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Xiubo Du has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Chao Wang
Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China
1 shared publication - Jing Tian
Department of Marine Biology, Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Shenzhen University, Shenzhen 518060, China
1 shared publication - Qiong Liu
Shenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, China
1 shared publication - Ruo-Ran Wang
College of Life Sciences, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen 518060, China
1 shared publication - Shi Qiu
College of Life Sciences, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen 518060, China
1 shared publication - Zhi Wang
Department of Marine Biology, Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Shenzhen University, Shenzhen 518060, China
1 shared publication
Latest Publications
- Open Access
- 6 June 2014
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 15 (6) , 10199-10214
Direct Interaction between Selenoprotein P and Tubulin
Selenium (Se), an essential trace element for human health, mainly exerts its biological function via selenoproteins. Among the 25 selenoproteins identified in human, selenoprotein P (SelP) is the only one that contains multiple selenocysteines (Sec) in the sequence, and has been suggested to function as a Se transporter. Upon feeding a selenium-deficient diet, mice lacking SelP develop severe neurological dysfunction and exhibit widespread brainstem neurodegeneration, indicating an important role of SelP in normal brain function. To further elucidate the function of SelP in the brain, SelP was screened by the yeast two-hybrid system from a human fetal brain cDNA library for interactive proteins. Our results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). The interaction between SelP and tubulin was verified by fluorescence resonance energy transfer (FRET) and co-immunoprecipitation (co-IP) assays. We further found that SelP interacts with the C-terminus of tubulin by its His-rich domain, as demonstrated by FRET and Isothermal Titration Calorimetry (ITC) assays. The implications of the interaction between SelP and tubulin in the brain and in Alzheimer’s disease are discussed.
- 6 June 2014
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 15 (6) , 10199-10214
Open AccessDirect Interaction between Selenoprotein P and Tubulin
Selenium (Se), an essential trace element for human health, mainly exerts its biological function via selenoproteins. Among the 25 selenoproteins identified in human, selenoprotein P (SelP) is the only one that contains multiple selenocysteines (Sec) in the sequence, and has been suggested to function as a Se transporter. Upon feeding a selenium-deficient diet, mice lacking SelP develop severe neurological dysfunction and exhibit widespread brainstem neurodegeneration, indicating an important role of SelP in normal brain function. To further elucidate the function of SelP in the brain, SelP was screened by the yeast two-hybrid system from a human fetal brain cDNA library for interactive proteins. Our results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). The interaction between SelP and tubulin was verified by fluorescence resonance energy transfer (FRET) and co-immunoprecipitation (co-IP) assays. We further found that SelP interacts with the C-terminus of tubulin by its His-rich domain, as demonstrated by FRET and Isothermal Titration Calorimetry (ITC) assays. The implications of the interaction between SelP and tubulin in the brain and in Alzheimer’s disease are discussed.