Phosphorylation of FAM134C by CK2 controls starvation-induced ER-phagy.

The article discusses research on the activation mechanism unique to FAM134C during starvation. In fed conditions, FAM134C is phosphorylated by casein kinase 2 at critical residues flanking the LC3-interacting region domain. During starvation, mTORC1 inhibition promotes receptor activation and endoplasmic reticulum (ER) via autophagy. Results show the physiological relevance of FAM134C phosphorylation during starvation-induced ER-phagy in liver lipid metabolism.