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DIMERIZATION AND PHOSPHORYLATION OF NIX REGULATES ITS FUNCTION AS MITOPHAGY RECEPTOR (CROSBI ID 616278)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa

Novak, Ivana ; Fischkin, Evgeni ; Hamacher-Brady, Anne ; Brady Nathan ; Đikić, Ivan DIMERIZATION AND PHOSPHORYLATION OF NIX REGULATES ITS FUNCTION AS MITOPHAGY RECEPTOR. 2011

Podaci o odgovornosti

Novak, Ivana ; Fischkin, Evgeni ; Hamacher-Brady, Anne ; Brady Nathan ; Đikić, Ivan

engleski

DIMERIZATION AND PHOSPHORYLATION OF NIX REGULATES ITS FUNCTION AS MITOPHAGY RECEPTOR

Recent discoveries of autophagic receptors that recognize specific cellular cargo have opened a new chapter in autophagy field. Selective removal of damaged organelles or protein aggregates is essential for the proper cellular homeostasis and survival. We have recently identified and characterized Nix/Bnip3L mitochondrial protein as mitophagy receptor that, in LIR-dependent manner, interacts with LC3/GABARAP proteins and recruits autophagy machinery to damaged mitochondria. Moreover, we have shown that Nix mediates mitochondrial clearance during reticulocyte differentiation. Additionally, Nix forms strong homodimers and we propose that Nix dimerization is required for the recruitment of LC3/GABARAP to damaged mitochondria and is a trigger for mitophagy. Recent discovery of Optn, an autophagy receptor involved in recognition of intracellular bacteria, showed that its autophagic function is regulated by phosphorylation of the LIR motif. We also show that phosphorylation of LIR motifs increases affinity of binding to LC3B, indicating that phosphorylation of mitophagy receptor Nix is involved in fine tuning of mitophagy.

mitophagy; autophagy; mitochondria

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Podaci o prilogu

2011.

nije evidentirano

objavljeno

Podaci o matičnoj publikaciji

Podaci o skupu

Autophagy in Health and Disease

predavanje

30.10.2011-04.11.2011

Ma'ale HaHamisha, Izrael

Povezanost rada

Biologija