RACK1 is an interaction partner of ATG5 and a novel regulator of autophagy
Erbil, Seçil and Oral, Özlem and Mitou, Geraldine and Kığ, Cenk and Durmaz, Emel and Güven-Maiorov, Emine and Gülaçtı, Ferah and Gökçe, Gökçen and Dengjel, Jön and Sezerman, Uğur and Gözüaçık, Devrim (2016) RACK1 is an interaction partner of ATG5 and a novel regulator of autophagy. Journal of Biological Chemistry . ISSN 0021-9258 (Print) 1083-351X (Online) Published Online First http://dx.doi.org/10.1074/jbc.M115.708081
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Official URL: http://dx.doi.org/10.1074/jbc.M115.708081
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 mTOR 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.
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