Emerging roles of HECT-type E3 ubiquitin ligases in autophagy regulation: Molecular Oncology

G. Melino, F. Cecconi, P.G. Pelicci, T.W. Mak, F. Bernassola

Research output: Contribution to journalArticle

Abstract

Autophagy is a conserved self-eating process that delivers cytoplasmic material to the lysosome to allow degradation of intracellular components, including soluble, unfolded and aggregated proteins, damaged organelles, and invading microorganisms. Autophagy provides a homeostatic control mechanism and is essential for balancing sources of energy in response to nutrient stress. Autophagic dysfunction or dysregulation has been implicated in several human pathologies, including cancer and neurodegeneration, and its modulation has substantial potential as a therapeutic strategy. Given the relevant clinical and therapeutic implications of autophagy, there is emerging intense interest in the identification of the key factors regulating the components of the autophagic machinery. Various post-translational modifications, including ubiquitylation, have been implicated in autophagy control. The list of the E3 ubiquitin protein ligases involved in the regulation of several steps of the autophagic process is continuously growing. In this review, we will focus on recent advances in the understanding of the role of the homologous to the E6AP carboxyl terminus-type E3 ubiquitin ligases in autophagy control. © 2019 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
Original languageEnglish
Pages (from-to)2033-2048
Number of pages16
JournalMol. Oncol.
Volume13
Issue number10
DOIs
Publication statusPublished - 2019

    Fingerprint

Keywords

  • autophagy
  • HECT E3 ubiquitin ligases
  • proteasomal degradation
  • ubiquitylation
  • cell protein
  • hect type e3 ubiquitin ligase
  • huwe1 protein
  • itch protein
  • nedd4 1 protein
  • nedd4 2 protein
  • proteasome
  • smurf1 protein
  • smurf2 protein
  • ubiquitin
  • ubiquitin protein ligase E3
  • unclassified drug
  • ww domain containing e3 ubiquitin protein ligase 1
  • carboxy terminal sequence
  • human
  • nonhuman
  • priority journal
  • protein domain
  • protein function
  • regulatory mechanism
  • Review
  • ubiquitination

Cite this