Direct Interaction between Selenoprotein P and Tubulin

International Journal of Molecular Sciences

Xiubo Du¹  Shi Qiu²  Zhi Wang¹  Ruoran Wang²  Chao Wang²  Jing Tian¹ 

[1] Department of Marine Biology, Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Shenzhen University, Shenzhen 518060, China; E-Mails:;College of Life Sciences, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen 518060, China; E-Mails:

关键词: selenoprotein P (SelP);    tubulin;    protein-protein interaction;    yeast two-hybrid system;    fluorescence resonance energy transfer (fret);   

DOI  :  10.3390/ijms150610199

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.