Logo image
The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
Journal article   Peer reviewed

The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1

H Plun-Favreau, K Klupsch, N Moisoi, S Gandhi, S Kjaer, D Frith, K Harvey, E Deas, Robert J Harvey, N McDonald, …
Nature Cell Biology, Vol.9(11), pp.1243-1252
2007
url
https://doi.org/10.1038/ncb1644View
Published Version

Abstract

In mice, targeted deletion of the serine protease HtrA2 (also known as Omi) causes mitochondrial dysfunction leading to a neurodegenerative disorder with parkinsonian features. In humans, point mutations in HtrA2 are a susceptibility factor for Parkinson's disease (PARK13 locus). Mutations in PINK1, a putative mitochondrial protein kinase, are associated with the PARK6 autosomal recessive locus for susceptibility to early-onset Parkinson's disease. Here we determine that HtrA2 interacts with PINK1 and that both are components of the same stress-sensing pathway. HtrA2 is phosphorylated on activation of the p38 pathway, occurring in a PINK1-dependent manner at a residue adjacent to a position found mutated in patients with Parkinson's disease. HtrA2 phosphorylation is decreased in brains of patients with Parkinson's disease carrying mutations in PINK1. We suggest that PINK1-dependent phosphorylation of HtrA2 might modulate its proteolytic activity, thereby contributing to an increased resistance of cells to mitochondrial stress.

Details

Metrics

1 File views/ downloads
198 Record Views

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Collaboration types
Domestic collaboration
Web Of Science research areas
Cell Biology

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

Source: InCites

Logo image