PINK1/Parkin Mediated Mitophagy, Ca2+ Signalling, and ER-Mitochondria Contacts in Parkinson's Disease

Int J Mol Sci. 2020 Mar 5;21(5):1772. doi: 10.3390/ijms21051772.

Abstract

Endoplasmic reticulum (ER)-mitochondria contact sites are critical structures for cellular function. They are implicated in a plethora of cellular processes, including Ca2+ signalling and mitophagy, the selective degradation of damaged mitochondria. Phosphatase and tensin homolog (PTEN)-induced kinase (PINK) and Parkin proteins, whose mutations are associated with familial forms of Parkinson's disease, are two of the best characterized mitophagy players. They accumulate at ER-mitochondria contact sites and modulate organelles crosstalk. Alterations in ER-mitochondria tethering are a common hallmark of many neurodegenerative diseases including Parkinson's disease. Here, we summarize the current knowledge on the involvement of PINK1 and Parkin at the ER-mitochondria contact sites and their role in the modulation of Ca2+ signalling and mitophagy.

Keywords: Ca2+; ER–mitochondria tethering; PINK1; Parkin; mitophagy.

Publication types

  • Review

MeSH terms

  • Animals
  • Calcium / metabolism*
  • Calcium Signaling*
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / pathology*
  • Humans
  • Mitochondria / metabolism
  • Mitochondria / pathology*
  • Mitophagy*
  • Parkinson Disease / metabolism
  • Parkinson Disease / pathology*
  • Ubiquitin-Protein Ligases / metabolism*

Substances

  • Ubiquitin-Protein Ligases
  • parkin protein
  • Calcium