1. Phosphorylation of FAM134C by CK2 controls starvation-induced ER-phagy.
- Author
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Di Lorenzo, Giorgia, Iavarone, Francescopaolo, Maddaluno, Marianna, Belén Plata-Gómez, Ana, Aureli, Simone, Quezada Meza, Camila Paz, Cinque, Laura, Palma, Alessandro, Reggio, Alessio, Cirillo, Carmine, Sacco, Francesca, Stolz, Alexandra, Napolitano, Gennaro, Marin, Oriano, Pinna, Lorenzo A., Ruzzene, Maria, Limongelli, Vittorio, Efeyan, Alejo, Grumati, Paolo, and Settembre, Carmine
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LYSOSOMES , *INSULIN receptors , *DOXYCYCLINE , *CELL adhesion molecules , *CRISPRS , *MOLECULAR dynamics - Abstract
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.
- Published
- 2022
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