Reversible and Irreversible Aggregation of Proteins from the FET Family: Influence of Repeats in Protein Chain on Its Aggregation Capacity

Author(s): Oxana V. Galzitskaya

Journal Name: Current Protein & Peptide Science

Volume 17 , Issue 4 , 2016


Become EABM
Become Reviewer
Call for Editor

Abstract:

The discovery of protein chain regions responsible for protein aggregation is an important result of studying of the molecular mechanisms of prion diseases and different proteinopathies associated with the formation of pathological aggregations through the prion mechanism. The ability to control aggregation of proteins could be an important tool in the arsenal of the drug development. Here we demonstrate, on an example of RNA-binding proteins of the FET family from six animal species (human, gorilla, pig, mouse, chicken, zebra fish), the possible role of repeats within the disordered regions. For these proteins, different repeats are revealed in the prion-like (N-terminal disordered) domains, and in the C-terminal disordered regions, predicted using bioinformatics methods. Moreover, we have found that in more complex organisms the number of repeats is increased. It can be hypothesized that the presence of a large number of repeats in the disordered regions in the proteins of the FET-family could both modulate and accelerate the formation of a dynamic cross-beta structure, and pathological aggregates.

Keywords: Amyotrophic lateral sclerosis, disordered regions, motifs of low complexity, proteinopathies, repeats.

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 17
ISSUE: 4
Year: 2016
Published on: 22 June, 2015
Page: [319 - 331]
Pages: 13
DOI: 10.2174/1389203716666150623103824
Price: $65

Article Metrics

PDF: 28
HTML: 4
EPUB: 1
PRC: 1