Reversible amyloid fiber formation in the N terminus of androgen receptor.
Fiche publication
Date publication
novembre 2014
Journal
Chembiochem : a European journal of chemical biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr CERALINE Jocelyn, Dr DELSUC Marc-André, Mr EBERLING Pascal , Dr NOMINE Yves
Tous les auteurs :
Asencio-Hernández J, Ruhlmann C, McEwen A, Eberling P, Nominé Y, Céraline J, Starck JP, Delsuc MA
Lien Pubmed
Résumé
Most of the biological effects of androgen hormones are mediated through an intracellular transcription factor, the androgen receptor (AR). This protein presents a long disordered N-terminal domain (NTD), known to aggregates into amyloid fibers.1 This aggregation property is usually associated with the presence of a poly-glutamine tract (polyQ), known to be involved in several pathologies.2 The NTD has gain interest recently because potential anti-prostate-cancer molecules could target this domain.3 Here, we characterize a conserved region of the NTD (distal from polyQ); it promotes the formation of amyloid fibers under mild oxidative conditions. Unlike most fibrils, which are irreversibly aggregated, the free peptides can be restored from the fibril by the addition of a reducing agent.
Mots clés
Amino Acid Sequence, Amyloid, chemistry, Circular Dichroism, Dimerization, Humans, Male, Microscopy, Electron, Molecular Sequence Data, Peptides, chemistry, Protein Structure, Secondary, Receptors, Androgen, chemistry
Référence
Chembiochem. 2014 Nov;15(16):2370-3