Erbil, Secil Oral, Ozlem Mitou, Geraldine Kig, Cenk Durmaz-Timucin, Emel Guven-Maiorov, Emine Gulacti, Ferah Gokce, Gokcen Dengjel, Jörn Sezerman, Osman Ugur Gozuacik, Devrim 2016-05-08 Autophagy is biological mechanism allowing recycling of long-lived proteins, abnormal protein aggregates, and damaged organelles under cellular stress conditions. Following sequestration in double- or multimembrane autophagic vesicles, the cargo is delivered to lysosomes for degradation. ATG5 is a key component of an E3-like ATG12-ATG5-ATG16 protein complex that catalyzes conjugation of the MAP1LC3 protein to lipids, thus controlling autophagic vesicle formation and expansion. Accumulating data indicate that ATG5 is a convergence point for autophagy regulation. Here, we describe the scaffold protein RACK1 (receptor activated C-kinase 1, GNB2L1) as a novel ATG5 interactor and an autophagy protein. Using several independent techniques, we showed that RACK1 interacted with ATG5. Importantly, classical autophagy inducers (starvation or mammalian target of rapamycin blockage) stimulated RACK1-ATG5 interaction. Knockdown of RACK1 or prevention of its binding to ATG5 using mutagenesis blocked autophagy activation. Therefore, the scaffold protein RACK1 is a new ATG5-interacting protein and an important and novel component of the autophagy pathways. application/pdf https://folia.unifr.ch/global/documents/305143 https://folia.unifr.ch/documents/305143/files/den_rip.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M115.708081 info:eu-repo/semantics/openAccess License undefined Journal of Biological Chemistry. - 2016, vol. 291, no. 32, p. 16753–16765 autophagy lysosome mammalian target of rapamycin (mTOR) protein-protein interaction signaling ATG12-5-16 ATG5 RACK1 p70S6K info:eu-repo/classification/udc/57 RACK1 is an interaction partner of ATG5 and a novel regulator of autophagy http://purl.org/coar/resource_type/c_6501