Ubiquitination and SUMOylation of Amyloid and Amyloid-like Proteins in Health and Disease

Curr Issues Mol Biol. 2020:35:195-230. doi: 10.21775/cimb.035.195. Epub 2019 Aug 18.

Abstract

Post-translational modifications (PTMs) play important roles in altering the structure and function of proteins. In this article, we focus on ubiquitination and SUMOylation of amyloidogenic proteins. We discuss the functional contributions of PTMs on proteins involved in amyloid-related diseases as well as the aberrant PTM signatures of the disease agents. In addition, we extend our discussion to the nascent field of functional amyloids, a subclass of amyloids that perform physiological functions. Here, we present examples from mammals and yeast to gain insight into physiological regulation of amyloid-like proteins.

Publication types

  • Review

MeSH terms

  • Alzheimer Disease / enzymology
  • Alzheimer Disease / metabolism*
  • Amyloidogenic Proteins / chemistry
  • Amyloidogenic Proteins / metabolism*
  • Amyloidogenic Proteins / toxicity
  • Amyotrophic Lateral Sclerosis / enzymology
  • Amyotrophic Lateral Sclerosis / metabolism*
  • Animals
  • Humans
  • Peptides / metabolism
  • Prions / chemistry
  • Prions / metabolism
  • Protein Processing, Post-Translational
  • Sumoylation*
  • Superoxide Dismutase-1 / chemistry
  • Superoxide Dismutase-1 / metabolism
  • Synucleinopathies / enzymology
  • Synucleinopathies / metabolism*
  • Ubiquitination*
  • Yeasts / genetics
  • Yeasts / metabolism
  • tau Proteins / chemistry
  • tau Proteins / metabolism

Substances

  • Amyloidogenic Proteins
  • Peptides
  • Prions
  • SOD1 protein, human
  • tau Proteins
  • polyglutamine
  • Superoxide Dismutase-1