Publication: Polyglutamined expanded androgen receptor interacts with chaperonin CCT
Issued Date
2012-11-01
Resource Type
ISSN
18780849
17697212
17697212
Other identifier(s)
2-s2.0-84867140090
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Mahidol University
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SCOPUS
Bibliographic Citation
European Journal of Medical Genetics. Vol.55, No.11 (2012), 599-604
Suggested Citation
Suttikarn Pongtepaditep, Thawornchai Limjindaporn, Patcharee Lertrit, Chatchawan Srisawat, Chanin Limwongse Polyglutamined expanded androgen receptor interacts with chaperonin CCT. European Journal of Medical Genetics. Vol.55, No.11 (2012), 599-604. doi:10.1016/j.ejmg.2012.06.013 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/13581
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Title
Polyglutamined expanded androgen receptor interacts with chaperonin CCT
Other Contributor(s)
Abstract
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. © 2012 Elsevier Masson SAS.