Naslov
Nix is a selective autophagy receptor for mitochondrial clearance

Autori
Novak, Ivana ; Kirkin, Vladimir ; McEwan, David ; Đikić, Ivan

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

Skup
At the joint edge of cellular microbiology and cell biology

Mjesto i datum
Kraków, Poljska, 09.10.2010. - 14.10.2010

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
nix; mitophagy; receptor

Sažetak
Most age-related diseases are characterized by the accumulation of aberrant protein suggesting a failure in the clearance of proteins targeted for degradation. Evolutionarily conserved process known as autophagy functions as an essential cytoprotective mechanism, which sequesters and destroys toxic cellular components including aggregated proteins or damaged organelles. The major challenge is to identify and functionally characterize molecular mechanisms that regulate these processes. Of particular interest are adaptor proteins that bind to ubiquitin and ubiquitin-like modifiers, LC3/GABARAP. The identification of specific autophagy receptors, such as p62 that can bind to both ubiquitin and Ubl modifiers, has provided a molecular link between ubiquitinated aggregates and an autophagic response. The Ubl modifiers are of particular interest due to their similarity to Ub, which has been identified as a common signaling component in various processes. We have identified another LC3/GABARAP interacting protein, called Nix (also known as BNIPL3), that localizes to the mitochondrial membrane and is a mitochondrial receptor for autophagy. We have characterized the interaction between LC3/GABARAP and Nix and determined the tetrapeptide sequence WxxL in Nix, as LC3-interacting region (LIR), essential for the interaction with LC3. We propose that Nix functions as a mitochondrial stress sensor by acting as an autophagy receptor for selective forms of mitophagy.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA