Kaleidoscopic protein-protein interactions in the life and death of ataxin-1: new strategies against protein aggregation

Trends Neurosci. 2014 Apr;37(4):211-8. doi: 10.1016/j.tins.2014.02.003. Epub 2014 Mar 11.

Abstract

Understanding how proteins protect themselves from aberrant aggregation is of primary interest for understanding basic biology, protein biochemistry, and human disease. We discuss the paradigmatic example of ataxin-1 (Atx1), the protein responsible for neurodegenerative spinocerebellar ataxia type 1 (SCA1). This disease is part of the increasing family of pathologies caused by protein aggregation and misfolding. We discuss the importance of protein-protein interactions not only in the nonpathological function of Atx1 but also in protecting the protein from aggregation and misfolding. The lessons learned from Atx1 may lead to a more general understanding of the cell's protective strategies against aggregation. The obtained knowledge may suggest a new perspective for designing specific therapeutic strategies for the cure of misfolding diseases.

Keywords: misfolding diseases; polyglutamine; protein aggregation; protein–protein interactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Ataxin-1
  • Ataxins
  • DNA Repeat Expansion
  • Drug Design
  • Heredodegenerative Disorders, Nervous System / drug therapy
  • Heredodegenerative Disorders, Nervous System / genetics
  • Heredodegenerative Disorders, Nervous System / metabolism
  • Humans
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Peptides / genetics
  • Peptides / metabolism
  • Protein Aggregates
  • Protein Aggregation, Pathological
  • Protein Folding
  • Protein Multimerization

Substances

  • ATXN1 protein, human
  • Ataxin-1
  • Ataxins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Peptides
  • Protein Aggregates
  • polyglutamine