13 research outputs found
GMAP is an Atg8a-interacting protein that regulates Golgi turnover in Drosophila
Selective autophagy receptors and adapters contain short linear motifs called LIR motifs (LC3-interacting re-
gion), which are required for the interaction with the Atg8-family proteins. LIR motifs bind to the hydrophobic
pockets of the LIR motif docking site (LDS) of the respective Atg8-family proteins. The physiological signif-
icance of LDS docking sites has not been clarified in vivo. Here, we show that Atg8a-LDS mutant Drosophila
flies accumulate autophagy substrates and have reduced lifespan. Using quantitative proteomics to identify
the proteins that accumulate in Atg8a-LDS mutants, we identify the cis-Golgi protein GMAP (Golgi microtu-
bule-associated protein) as a LIR motif-containing protein that interacts with Atg8a. GMAP LIR mutant flies
exhibit accumulation of Golgi markers and elongated Golgi morphology. Our data suggest that GMAP medi-
ates the turnover of Golgi by selective autophagy to regulate its morphology and size via its LIR motif-medi-
ated interaction with Atg8a
RNS vakcinák humán felhasználása napjainkban
INST: L_200A COVID-19 pandémia árnyékában napjaink egyik legjobban kutatott területe az új védőoltások előállítása, új és hatékony módszerek kifejlesztése a járványok megelőzésére és tovább-terjedésének megakadályozására
Az enyhe és középsúlyos-súlyos psoriasisos betegek összehasonlító jellemzése hazánkban = Comparative description of mild and moderate-to-severe psoriatic patients in Hungary
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Selective autophagy and Golgi quality control in Drosophila
The LIR motif-docking site (LDS) of Atg8/LC3 proteins is essential for the binding of LC3-interacting region (LIR)-containing proteins and their subsequent degradation by macroautophagy/autophagy. In our recent study, we created a mutated LDS site in Atg8a, the Drosophila homolog of Atg8/LC3 and found that LDS mutants accumulate known autophagy substrates and have reduced lifespan. We also conducted quantitative proteomics analyses and identified several proteins that are enriched in the LDS mutants, including Gmap (Golgi microtubule-associated protein). Gmap contains a LIR motif and accumulates in LDS mutants. We showed that Gmap and Atg8a interact in a LIR-LDS dependent manner and that the Golgi size and morphology are altered in Atg8a-LDS and Gmap-LIR motif mutants. Our findings highlight a role for Gmap in the regulation of Golgiphagy
Fiatalkorban és időskorban kialakuló psoriasis jellemzői a Debrecenben gondozott populációban
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