Fiche publication
Date publication
juin 2017
Journal
Biomolecules
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KIEFFER Bruno
,
Dr DELSUC Marc-André
Tous les auteurs :
Oppong E, Stier G, Gaal M, Seeger R, Stoeck M, Delsuc MA, Cato ACB, Kieffer B
Lien Pubmed
Résumé
The human androgen receptor (AR) is a ligand inducible transcription factor that harbors an amino terminal domain (AR-NTD) with a ligand-independent activation function. AR-NTD is intrinsically disordered and displays aggregation properties conferred by the presence of a poly-glutamine (polyQ) sequence. The length of the polyQ sequence as well as its adjacent sequence motifs modulate this aggregation property. AR-NTD also contains a conserved KELCKAVSVSM sequence motif that displays an intrinsic property to form amyloid fibrils under mild oxidative conditions. As peptide sequences with intrinsic oligomerization properties are reported to have an impact on the aggregation of polyQ tracts, we determined the effect of the KELCKAVSVSM on the polyQ stretch in the context of the AR-NTD using atomic force microscopy (AFM). Here, we present evidence for a crosstalk between the amyloidogenic properties of the KELCKAVSVSM motif and the polyQ stretch at the AR-NTD.
Mots clés
aggregation, amyloid peptides, androgen receptor, atomic force microscopy, nuclear receptor
Référence
Biomolecules. 2017 Jun 19;7(2):
