ArticleInternational journal of molecular sciences2014
Direct interaction between selenoprotein P and tubulin.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Selenoproteins: Zoom-In to Their Metal-Binding Properties in Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- The Role of Gut Microbiota in the Neuroprotective Effects of Selenium in Alzheimer's Disease.Molecular neurobiology · 2025Review
- Article
- "Alphabet" Selenoproteins: Implications in Pathology.International journal of molecular sciences · 2023Review
- Dietary Selenomethionine Reduce Mercury Tissue Levels and Modulate Methylmercury Induced Proteomic and Transcriptomic Alterations in Hippocampi of Adolescent BALB/c Mice.International journal of molecular sciences · 2022Article
- Roles of Selenoproteins in Brain Function and the Potential Mechanism of Selenium in Alzheimer's Disease.Frontiers in neuroscience · 2021Review
- Insights into the Potential Role of Mercury in Alzheimer's Disease.Journal of molecular neuroscience : MN · 2019Review
- The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism.Nutrition & metabolism · 2018Article
- Treatment strategies in Alzheimer's disease: a review with focus on selenium supplementation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016Review
- Selenium in the Therapy of Neurological Diseases. Where is it Going?Current neuropharmacology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.