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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 functi...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100148/ https://www.ncbi.nlm.nih.gov/pubmed/24914767 http://dx.doi.org/10.3390/ijms150610199 |
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author | Du, Xiubo Qiu, Shi Wang, Zhi Wang, Ruoran Wang, Chao Tian, Jing Liu, Qiong |
author_facet | Du, Xiubo Qiu, Shi Wang, Zhi Wang, Ruoran Wang, Chao Tian, Jing Liu, Qiong |
author_sort | Du, Xiubo |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4100148 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-41001482014-07-16 Direct Interaction between Selenoprotein P and Tubulin Du, Xiubo Qiu, Shi Wang, Zhi Wang, Ruoran Wang, Chao Tian, Jing Liu, Qiong Int J Mol Sci Article 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. MDPI 2014-06-06 /pmc/articles/PMC4100148/ /pubmed/24914767 http://dx.doi.org/10.3390/ijms150610199 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Du, Xiubo Qiu, Shi Wang, Zhi Wang, Ruoran Wang, Chao Tian, Jing Liu, Qiong Direct Interaction between Selenoprotein P and Tubulin |
title | Direct Interaction between Selenoprotein P and Tubulin |
title_full | Direct Interaction between Selenoprotein P and Tubulin |
title_fullStr | Direct Interaction between Selenoprotein P and Tubulin |
title_full_unstemmed | Direct Interaction between Selenoprotein P and Tubulin |
title_short | Direct Interaction between Selenoprotein P and Tubulin |
title_sort | direct interaction between selenoprotein p and tubulin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4100148/ https://www.ncbi.nlm.nih.gov/pubmed/24914767 http://dx.doi.org/10.3390/ijms150610199 |
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