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Nix is a selective autophagy receptor for mitochondrial clearance
Author(s) -
Novak Ivana,
Kirkin Vladimir,
McEwan David G,
Zhang Ji,
Wild Philipp,
Rozenknop Alexis,
Rogov Vladimir,
Löhr Frank,
Popovic Doris,
Occhipinti Angelo,
Reichert Andreas S,
Terzic Janos,
Dötsch Volker,
Ney Paul A,
Dikic Ivan
Publication year - 2010
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 - 10.1038/embor.2009.256
Subject(s) - autophagy , microbiology and biotechnology , ulk1 , cytosol , lysosome , mitochondrion , organelle , biology , receptor , mitophagy , ubiquitin , biochemistry , apoptosis , enzyme , gene , protein kinase a , phosphorylation , ampk
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy mediates selective removal of protein aggregates, organelles and microbes in cells. Yet, the specificity in targeting a particular substrate to the autophagy pathway remains poorly understood. Here, we show that the mitochondrial protein Nix is a selective autophagy receptor by binding to LC3/GABARAP proteins, ubiquitin‐like modifiers that are required for the growth of autophagosomal membranes. In cultured cells, Nix recruits GABARAP‐L1 to damaged mitochondria through its amino‐terminal LC3‐interacting region. Furthermore, ablation of the Nix:LC3/GABARAP interaction retards mitochondrial clearance in maturing murine reticulocytes. Thus, Nix functions as an autophagy receptor, which mediates mitochondrial clearance after mitochondrial damage and during erythrocyte differentiation.