Journal article

Inclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation

Mona Radwan, Jordan Lilley, Ching-Seng Ang, Gavin Reid, Danny Hatters

Published : 2020

Abstract

ABSTRACT Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and both have been reported to form an amyloid-like structure suggesting they might aggregate via similar mechanisms to confer cellular dysfunction similarly. Here we investigated which endogenous proteins were enriched in these inclusions and whether aggregation-prone lengths of polyQ (Q 97 ), in context of Huntingtin exon 1, shared similar patterns to aggregation-prone lengths of polyGA (101 GA..

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University of Melbourne Researchers