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Reversible Amyloid Fiber Formation in the N Terminus of Androgen Receptor
Author(s) -
AsencioHernández Julia,
Ruhlmann Christine,
McEwen Alastair,
Eberling Pascal,
Nominé Yves,
Céraline Jocelyn,
Starck JeanPhilippe,
Delsuc MarcAndré
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402420
Subject(s) - androgen receptor , chemistry , prostate cancer , amyloid (mycology) , receptor , amyloid fibril , androgen , biophysics , intracellular , microbiology and biotechnology , peptide , fibril , transcription factor , biochemistry , hormone , biology , medicine , amyloid β , gene , cancer , genetics , inorganic chemistry , disease
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.