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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
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Direct interaction between selenoprotein P and tubulin.
Xiubo Du1, Shi Qiu2, Zhi Wang3
1Department of Marine Biology, Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Shenzhen University, Shenzhen 518060, China. xiubo.du@gmail.com.
International Journal of Molecular Sciences
|June 11, 2014
Summary
Selenoprotein P (SelP), a key selenium transporter, interacts with tubulin in the brain. This discovery sheds light on SelP
Area of Science:
- Biochemistry
- Neuroscience
- Trace Element Metabolism
Background:
- Selenium (Se) is vital for human health, primarily through selenoproteins.
- Selenoprotein P (SelP) is unique among selenoproteins for its role as a potential selenium transporter.
- SelP deficiency in mice causes severe neurological dysfunction and brainstem neurodegeneration.
Purpose of the Study:
- To investigate the function of Selenoprotein P (SelP) within the brain.
- To identify proteins that interact with SelP in the human brain.
Main Methods:
- Yeast two-hybrid screening of a human fetal brain cDNA library.
- Fluorescence resonance energy transfer (FRET) assays.
- Co-immunoprecipitation (co-IP) assays.
- Isothermal Titration Calorimetry (ITC) assays.
Main Results:
- Selenoprotein P (SelP) was found to interact with tubulin, alpha 1a (TUBA1A).
- The interaction was confirmed using FRET and co-IP.
- SelP binds to the C-terminus of tubulin via its His-rich domain, verified by FRET and ITC.
Conclusions:
- SelP interacts with tubulin in the brain.
- This interaction may have implications for brain function and neurodegenerative diseases like Alzheimer's disease.
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