Autophagy-related protein 13 (ATG13)

Autophagy-related protein 13 (ATG13) is a conserved scaffold protein critical for the initiation of autophagy, a cellular process responsible for degrading and recycling cytoplasmic content. ATG13 is part of the ULK/Atg1 kinase complex in mammals and yeast, respectively, where it mediates the assembly and stability of the autophagy initiation machinery[3]. It contains an N-terminal HORMA domain necessary for recruitment of the class III PI 3-kinase complex via Atg14 and for the regulation of autophagic activity by nutrient signals[1]. The interaction of ATG13 with other complex components, such as ULK1 (mammals) or Atg1 (yeast) and FIP200/Atg17, is regulated by phosphorylation events mediated by the nutrient-responsive kinase TOR/mTOR, controlling the switch between growth and starvation-induced autophagy[2][3]. Dysfunction or altered regulation of ATG13 and its associated autophagy pathway has been implicated in cancer and neurodegenerative disorders. While ATG13 is central in autophagy, current pharmacological interventions act via upstream modulators rather than direct targeting of ATG13.

Other names

ATG13KIAA0652PARATARG8autophagy-related protein 13 homolog

Agents targeting the mTOR pathway (e.g., rapamycin) upregulate ATG13 dephosphorylation and promote autophagy[2]. No direct ATG13-targeting drugs currently known; intervention is typically indirect via upstream kinases.