LIR and APEAR, two distinct Atg8-binding features within Atg4
نویسندگان
چکیده
منابع مشابه
LIR and APEAR, two distinct Atg8-binding features within Atg4
During autophagy, double membrane vesicles called autophagosomes, engulf intracellular structures and deliver them to the vacuole/lysosome for degradation. In addition to its key role in maintaining metabolic homeostasis, autophagy is crucial in eliminating defective or superfluous cellular structures, and consequently impairments in this catabolic pathway cause various diseases. Central compon...
متن کاملConserved Atg8 recognition sites mediate Atg4 association with autophagosomal membranes and Atg8 deconjugation.
Deconjugation of the Atg8/LC3 protein family members from phosphatidylethanolamine (PE) by Atg4 proteases is essential for autophagy progression, but how this event is regulated remains to be understood. Here, we show that yeast Atg4 is recruited onto autophagosomal membranes by direct binding to Atg8 via two evolutionarily conserved Atg8 recognition sites, a classical LC3-interacting region (L...
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Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE). Atg8 functions in the formation of double-membrane autophagosomes, a central step in the well-co...
متن کاملAtg4 in autophagosome biogenesis
Double-membrane autophagosomes are the hallmark of autophagy, a catabolic process conserved among eukaryotes. Autophagy is crucial for the degradation of unwanted structures such as unfolded proteins, protein aggregates and dysfunctional organelles, which, if accumulated, could impair cellular homeostasis. Hence, autophagy dysregulation leads to the development of several pathologies including ...
متن کاملPI3P binding by Atg21 organises Atg8 lipidation.
Autophagosome biogenesis requires two ubiquitin-like conjugation systems. One couples ubiquitin-like Atg8 to phosphatidylethanolamine, and the other couples ubiquitin-like Atg12 to Atg5. Atg12~Atg5 then forms a heterodimer with Atg16. Membrane recruitment of the Atg12~Atg5/Atg16 complex defines the Atg8 lipidation site. Lipidation requires a PI3P-containing precursor. How PI3P is sensed and use...
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ژورنال
عنوان ژورنال: Oncotarget
سال: 2017
ISSN: 1949-2553
DOI: 10.18632/oncotarget.17697