| Background |
Atg101 was discovered as a binding protein for Atg13, a component of the ULK1 serine-threonine kinase complex required for autophagy. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. It is generally activated by conditions of nutrient deprivation, but is also associated with a number of physiological processes, including development, differentiation, neurodegeneration, infection, and cancer. The molecular machinery of autophagy was largely discovered in yeast and is directed by a number of autophagy-related (Atg) genes. The ULK1 complex includes both Atg13 and FIP200 and is required for starvation-induced autophagy. Interaction between Atg101 and Atg13 can be important for the stability and basal phosphorylation of Atg13 and ULK1. Atg101 has been reported to be phosphorylated at Ser11 by ULK1.
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