Polyglutamined expanded androgen receptor interacts with chaperonin CCT
| Autor: | Thawornchai Limjindaporn, Chanin Limwongse, Suttikarn Pongtepaditep, Patcharee Lertrit, Chatchawan Srisawat |
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| Rok vydání: | 2012 |
| Předmět: |
Adult
Male Huntingtin genetic structures Protein subunit Nerve Tissue Proteins macromolecular substances Biology Chaperonin Two-Hybrid System Techniques Genetics Huntingtin Protein Humans Receptor Genetics (clinical) HEK 293 cells General Medicine Molecular biology Muscular Disorders Atrophic eye diseases Cell biology Androgen receptor enzymes and coenzymes (carbohydrates) HEK293 Cells Receptors Androgen Protein folding sense organs Peptides Chaperonin Containing TCP-1 |
| Zdroj: | European Journal of Medical Genetics. 55:599-604 |
| ISSN: | 1769-7212 |
| Popis: | CCT chaperonin is a highly conserved molecular chaperone, which plays an important role in the folding of complex proteins in mammalian cells. CCT chaperonin interacts with huntingtin and results in decrease of aggregate formation followed by increase of cell survival. Using yeast-two-hybrid system, we screen for specific CCT chaperonin subunit, which can recognize and bind to androgen receptor. We show that subunit 6 of CCT chaperonin interacts with androgen receptor. Interestingly, CCT chaperonin shows higher binding affinity to polyglutamine expanded androgen receptor than that of the wild-type. We prove this interaction in mammalian cell models, which show co-localization of androgen receptor and subunit 6 of CCT in cellular cytosol. Therefore, not only huntingtin but also androgen receptor is a polyglutamine expanded protein, which is a substrate of CCT chaperonin. Our results suggest that CCT might play an essential role in modulation of folding of polyglutamine expanded proteins and could be another target for further therapeutic studies. |
| Databáze: | OpenAIRE |
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