title: Reversible amyloid fiber formation in the N terminus of androgen receptor.
abstract: 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.
authors.affiliation: Institut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM, U596, CNRS, UMR-7104, Université de Strasbourg, 1 rue Laurent Fries, 67404 Illkirch-Graffenstaden (France); NMRTEC S.A.S. Boulevard Sébastien Brandt, Bioparc, Bât. B, 67400 Illkirch-Graffenstaden (France).
authors.forename: Julia
authors.initials: J
authors.lastname: Asencio-Hernández
authors.forename: Christine
authors.initials: C
authors.lastname: Ruhlmann
authors.forename: Alastair
authors.initials: A
authors.lastname: McEwen
authors.forename: Pascal
authors.initials: P
authors.lastname: Eberling
authors.forename: Yves
authors.initials: Y
authors.lastname: Nominé
authors.forename: Jocelyn
authors.initials: J
authors.lastname: Céraline
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Starck
authors.forename: Marc-André
authors.initials: MA
authors.lastname: Delsuc
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D002942:Circular Dichroism; D019281:Dimerization; D006801:Humans; D008297:Male; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D011944:Receptors, Androgen / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000682:Amyloid; D010455:Peptides; D011944:Receptors, Androgen; C097188:polyglutamine
keywords: amyloid beta-peptides; androgen receptor; dimerization; disulfide bridge; self-assembly