دورية أكاديمية

F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics.

التفاصيل البيبلوغرافية
العنوان: F-actin binding regions on the androgen receptor and huntingtin increase aggregation and alter aggregate characteristics.
المؤلفون: Suzanne Angeli, Jieya Shao, Marc I Diamond
المصدر: PLoS ONE, Vol 5, Iss 2, p e9053 (2010)
بيانات النشر: Public Library of Science (PLoS), 2010.
سنة النشر: 2010
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Protein aggregation is associated with neurodegeneration. Polyglutamine expansion diseases such as spinobulbar muscular atrophy and Huntington disease feature proteins that are destabilized by an expanded polyglutamine tract in their N-termini. It has previously been reported that intracellular aggregation of these target proteins, the androgen receptor (AR) and huntingtin (Htt), is modulated by actin-regulatory pathways. Sequences that flank the polyglutamine tract of AR and Htt might influence protein aggregation and toxicity through protein-protein interactions, but this has not been studied in detail. Here we have evaluated an N-terminal 127 amino acid fragment of AR and Htt exon 1. The first 50 amino acids of ARN127 and the first 14 amino acids of Htt exon 1 mediate binding to filamentous actin in vitro. Deletion of these actin-binding regions renders the polyglutamine-expanded forms of ARN127 and Htt exon 1 less aggregation-prone, and increases the SDS-solubility of aggregates that do form. These regions thus appear to alter the aggregation frequency and type of polyglutamine-induced aggregation. These findings highlight the importance of flanking sequences in determining the propensity of unstable proteins to misfold.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC2816219?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0009053
URL الوصول: https://doaj.org/article/d945fba450484987ab86ae214cd0b203
رقم الأكسشن: edsdoj.945fba450484987ab86ae214cd0b203
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0009053