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PTEN-L puts a brake on mitophagy.

Liming Wang1, Jigang Wang1, Yancheng Tang2

  • 1a Department of Physiology, Yong Loo Lin School of Medicine , National University of Singapore , Singapore.

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|August 15, 2018
PubMed
Summary

PTEN-L is a novel negative regulator of mitophagy. It dephosphorylates ubiquitin, preventing PINK1 and PRKN recruitment and activity, thus acting as a brake on this cellular degradation process.

Keywords:
MitophagyPRKNPTEN-Lphosphataseubiquitin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Mitophagy selectively degrades damaged mitochondria via the autophagic pathway.
  • The PTEN induced putative kinase 1 (PINK1) and parkin RBR E3 ubiquitin protein ligase (PRKN) pathway regulates mitophagy through ubiquitin phosphorylation (p-Ser65-Ub).
  • The existence of a phosphatase counteracting PINK1-mediated ubiquitin phosphorylation was unknown.

Purpose of the Study:

  • To identify novel regulators of mitophagy.
  • To investigate the role of PTEN-L in mitophagy.
  • To elucidate the mechanism by which PTEN-L regulates mitophagy.

Main Methods:

  • Localization studies of PTEN-L at the mitochondria.
  • Assessment of PRKN translocation and phosphorylation.
  • Evaluation of PRKN E3 ligase activity.
  • Analysis of p-Ser65-Ub levels.
  • Functional assays to determine mitophagy regulation.

Main Results:

  • PTEN-L localizes to the outer mitochondrial membrane.
  • PTEN-L inhibits PRKN mitochondrial translocation and phosphorylation.
  • PTEN-L impairs PRKN E3 ligase activity and maintains PRKN in an inactive state.
  • PTEN-L dephosphorylates p-Ser65-Ub, disrupting the mitophagy feedforward mechanism.
  • PTEN-L acts as a negative regulator of mitophagy.

Conclusions:

  • PTEN-L is a novel negative regulator of mitophagy.
  • PTEN-L functions by dephosphorylating p-Ser65-Ub, thereby inhibiting the PINK1-PRKN pathway.
  • PTEN-L acts as a crucial brake in the intricate regulation of mitophagy.