ULK1 ubiquitylation is regulated by phosphorylation on its carboxy terminus

Research output: Contribution to journalComment/debate

2 Citations (Scopus)

Abstract

Autophagy is a highly conserved process that acts sequestering cytoplasmic components for their degradation by the lysosomes. It consists of several sequential steps that have to be finely regulated to ensure both its progression and termination. Post-translational modifications (PTMs) play an important role in regulating ATG proteins function in different stages of autophagy. Recently, we demonstrated that, during prolonged starvation, ULK1 protein is specifically ubiquitylated by NEDD4L, and that this regulation is important to protect cells against excessive autophagy. In this Extra view, we show that ULK1 phosphorylation at 3 different sites on the same ULK1 target region for NEDD4L is preparatory for its ubiquitylation and subsequent degradation. This adds to the complexity of ULK1 multi-level regulation by several factors, including kinases, phosphatases and acetylases, with each contributing to autophagy homeostasis.

Original languageEnglish
Pages (from-to)1744-1747
Number of pages4
JournalCell Cycle
Volume16
Issue number19
DOIs
Publication statusPublished - Oct 2 2017

Fingerprint

Ubiquitination
Autophagy
Phosphorylation
Acetylesterase
Post Translational Protein Processing
Starvation
Lysosomes
Phosphoric Monoester Hydrolases
Homeostasis
Phosphotransferases
Proteins

Keywords

  • autophagy
  • kinases
  • ubiquitin
  • ubiquitin ligases

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

Cite this

ULK1 ubiquitylation is regulated by phosphorylation on its carboxy terminus. / Nazio, Francesca; Carinci, Marianna; Cecconi, Francesco.

In: Cell Cycle, Vol. 16, No. 19, 02.10.2017, p. 1744-1747.

Research output: Contribution to journalComment/debate

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