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Int. J. Mol. Sci. 2014, 15(6), 10199-10214; doi:10.3390/ijms150610199
Article

Direct Interaction between Selenoprotein P and Tubulin

1,†
, 2,†
, 1
, 2
, 2
, 1
 and 1,*
Received: 19 March 2014; in revised form: 12 May 2014 / Accepted: 23 May 2014 / Published: 6 June 2014
(This article belongs to the collection Proteins and Protein-Ligand Interactions)
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Abstract: 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.
Keywords: selenoprotein P (SelP); tubulin; protein-protein interaction; yeast two-hybrid system; fluorescence resonance energy transfer (fret) selenoprotein P (SelP); tubulin; protein-protein interaction; yeast two-hybrid system; fluorescence resonance energy transfer (fret)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Du, X.; Qiu, S.; Wang, Z.; Wang, R.; Wang, C.; Tian, J.; Liu, Q. Direct Interaction between Selenoprotein P and Tubulin. Int. J. Mol. Sci. 2014, 15, 10199-10214.

AMA Style

Du X, Qiu S, Wang Z, Wang R, Wang C, Tian J, Liu Q. Direct Interaction between Selenoprotein P and Tubulin. International Journal of Molecular Sciences. 2014; 15(6):10199-10214.

Chicago/Turabian Style

Du, Xiubo; Qiu, Shi; Wang, Zhi; Wang, Ruoran; Wang, Chao; Tian, Jing; Liu, Qiong. 2014. "Direct Interaction between Selenoprotein P and Tubulin." Int. J. Mol. Sci. 15, no. 6: 10199-10214.


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