| Title: |
Reversible Amyloid Fiber Formation in the N Terminus of Androgen Receptor |
| Authors: |
Asencio-Hernández, Julia; Ruhlmann, Christine; McEwen, Alastair; Eberling, Pascal; Nominé, Yves; Céraline, Jocelyn; Starck, Jean‐philippe; Delsuc, Marc‐andré |
| Contributors: |
Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC); Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS); Biotechnologie et signalisation cellulaire (BSC); Université de Strasbourg (UNISTRA)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS)-Centre National de la Recherche Scientifique (CNRS); Interface de Recherche Fondamentale et Appliquée en Cancérologie (IRFAC - Inserm U1113); Centre Paul Strauss (CRLCC Paul Strauss); UNICANCER-UNICANCER-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Fédération de Médecine Translationelle de Strasbourg (FMTS); NMRTEC |
| Source: |
ISSN: 1439-4227. |
| Publisher Information: |
HAL CCSD; Wiley-VCH Verlag |
| Publication Year: |
2014 |
| Collection: |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
| Subject Terms: |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry; Molecular Biology |
| Description: |
International audience ; 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. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
hal-04295904; https://hal.science/hal-04295904 |
| DOI: |
10.1002/cbic.201402420 |
| Availability: |
https://hal.science/hal-04295904; https://doi.org/10.1002/cbic.201402420 |
| Accession Number: |
edsbas.FDA94B6D |
| Database: |
BASE |