Elevated ATG13 in serum of patients with ME/CFS stimulates oxidative stress response in microglial cells via activation of receptor for advanced glycation end products (RAGE).
Klotho-mediated changes in the expression of Atg13 alter formation of ULK1 complex and thus initiation of ER- and Golgi-stress response mediated autophagy.
these results demonstrate the effective anti-autophagic of NRAGE in non-small-cell lung cancer cells through AMPK/Ulk1/Atg13 autophagy signaling pathways. Therefore NRAGE could be used as a potential therapeutic target for lung cancer.
These results show that the SiMoA technology can detect quantitatively low levels of endogenous biomarkers with the ability to detect the loss of pSer(318)-Atg13 upon ULK1 inhibition.
In response to DNA damage ULK1 and ULK2 are upregulated by p53. The upregulation of ULK1 (ULK2)/ATG13 complex by p53 is necessary for the sustained autophagy activity induced by DNA damage.
Studies elucidated the inhibitory mechanism in which mTORC1 phosphorylates the autophagy regulatory complex containing unc-51-like kinase 1 (ULK1) the mammalian Atg13 protein and focal adhesion kinase interacting protein of 200 kD (FIP200).
The identification of the novel protein Atg101 and the validation of Atg13 and Atg101 as ULK1-interacting proteins suggests an Atg1 complex is involved in the induction of macroautophagy in mammalian cells.
ATG13 and ULK1 are phosphorylated by the mTOR pathway in a nutrient starvation-regulated manner indicating that the ULK1.ATG13.FIP200 complex acts as a node for integrating incoming autophagy signals into autophagosome biogenesis.
The functions of ULK1 and ULK2 are controlled by autophosphorylation and conformational changes involving exposure of the C-terminal domain and interaction with the putative human homologue of Atg13; The gene product is the functional homologue of yeast Atg13 and required for autophagy in mammalian cells.
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