Mitochondrial E3 ubiquitin ligase parkin: Relationships with other causal proteins in familial parkinson’s disease and its substrate-involved mouse experimental models

Satoru Torii, Shuya Kasai, Tatsushi Yoshida, Ken Ichi Yasumoto, Shigeomi Shimizu

Research output: Contribution to journalReview articlepeer-review

2 Citations (Scopus)

Abstract

Parkinson’s disease (PD) is a common neurodegenerative disorder. Recent identification of genes linked to familial forms of PD has revealed that post-translational modifications, such as phosphorylation and ubiquitination of proteins, are key factors in disease pathogenesis. In PD, E3 ubiquitin ligase Parkin and the serine/threonine-protein kinase PTEN-induced kinase 1 (PINK1) mediate the mitophagy pathway for mitochondrial quality control via phosphorylation and ubiquitination of their substrates. In this review, we first focus on well-characterized PINK1 phosphorylation motifs. Second, we describe our findings concerning relationships between Parkin and HtrA2/Omi, a protein involved in familial PD. Third, we describe our findings regarding inhibitory PAS (Per/Arnt/Sim) domain protein (IPAS), a member of PINK1 and Parkin substrates, involved in neurodegeneration during PD. IPAS is a dual-function protein involved in transcriptional repression of hypoxic responses and the pro-apoptotic activities.

Original languageEnglish
Article number1202
JournalInternational journal of molecular sciences
Volume21
Issue number4
DOIs
Publication statusPublished - 2020 Feb 2

Keywords

  • 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)
  • HtrA2/Omi
  • IPAS
  • PINK1
  • Parkin
  • Parkinson’s disease

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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