Naslov
DIMERIZATION AND PHOSPHORYLATION OF NIX REGULATES ITS FUNCTION AS MITOPHAGY RECEPTOR

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

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Skup
Autophagy in Health and Disease

Mjesto i datum
Ma'ale HaHamisha, Izrael, 30.10.2011. - 04.11.2011

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
mitophagy; autophagy; mitochondria

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA