학술논문
Phosphorylation of FAM134C by CK2 controls starvation-induced ER-phagy.
Document Type
Article
Author
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; Settembre, Carmine
Source
Subject
*LYSOSOMES
*INSULIN receptors
*DOXYCYCLINE
*CELL adhesion molecules
*CRISPRS
*MOLECULAR dynamics
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Language
ISSN
2375-2548
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.