Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules2017, 7, 44.
Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules 2017, 7, 44.
Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules2017, 7, 44.
Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules 2017, 7, 44.
Abstract
The human androgen receptor (AR) is a ligand inducible transcription factor harboring an amino terminal domain (AR-NTD) hosting the ligand independent activation function. AR-NTD is intrinsically disordered and display aggregation properties conferred by the presence of a poly-glutamine (polyQ) sequence of 22 residues. The length of the polyQ sequence, as well as the presence of adjacent sequence motifs modulate this aggregation property. AR-NTD contains also a conserved sequence motif KELCKAVSVSM that displays an intrinsic property to form amyloid fibrils under mild oxidative conditions of its conserved cysteine residue. As peptide sequences with intrinsic ability to oligomerize are reported to have an impact on the aggregation of polyQ tract, 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.
Keywords
amyloid peptides; androgen receptor; nuclear receptor; aggregation; atomic force microscopy
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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