Ontology highlight
ABSTRACT:
SUBMITTER: Boeddrich A
PROVIDER: S-EPMC1440312 | biostudies-literature | 2006 Apr
REPOSITORIES: biostudies-literature
Boeddrich Annett A Gaumer Sébastien S Haacke Annette A Tzvetkov Nikolay N Albrecht Mario M Evert Bernd O BO Müller Eva C EC Lurz Rudi R Breuer Peter P Schugardt Nancy N Plassmann Stephanie S Xu Kexiang K Warrick John M JM Suopanki Jaana J Wüllner Ullrich U Frank Ronald R Hartl Ulrich F UF Bonini Nancy M NM Wanker Erich E EE
The EMBO journal 20060309 7
Arginine/lysine-rich motifs typically function as targeting signals for the translocation of proteins to the nucleus. Here, we demonstrate that such a motif consisting of four basic amino acids in the polyglutamine protein ataxin-3 (Atx-3) serves as a recognition site for the interaction with the molecular chaperone VCP. Through this interaction, VCP modulates the fibrillogenesis of pathogenic forms of Atx-3 in a concentration-dependent manner, with low concentrations of VCP stimulating fibrillo ...[more]