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Cytosolic cleaved PINK 1 represses P arkin translocation to mitochondria and mitophagy
Author(s) -
Fedorowicz Maja A.,
VriesSchneider Rosa L. A.,
Rüb Cornelia,
Becker Dorothea,
Huang Yong,
Zhou Chun,
Alessi Wolken Dana M.,
Voos Wolfgang,
Liu Yuhui,
Przedborski Serge
Publication year - 2014
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1002/embr.201337294
Subject(s) - columbia university , library science , biology , sociology , computer science , media studies
PINK 1 is a mitochondrial kinase proposed to have a role in the pathogenesis of Parkinson's disease through the regulation of mitophagy. Here, we show that the PINK 1 main cleavage product, PINK 1 52, after being generated inside mitochondria, can exit these organelles and localize to the cytosol, where it is not only destined for degradation by the proteasome but binds to Parkin. The interaction of cytosolic PINK 1 with Parkin represses Parkin translocation to the mitochondria and subsequent mitophagy. Our work therefore highlights the existence of two cellular pools of PINK 1 that have different effects on Parkin translocation and mitophagy.