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RACK1 Is an Interaction Partner of ATG5 and a Novel Regulator of Autophagy.

  • Erbil S From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Oral O From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Mitou G From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Kig C From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Durmaz-Timucin E From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Guven-Maiorov E the Department of Chemical and Biological Engineering and Center for Computational Biology and Bioinformatics, Koc University, 34450 Istanbul, Turkey.
  • Gulacti F From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Gokce G From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey.
  • Dengjel J the Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland, and.
  • Sezerman OU the Department of Biostatistics and Medical Informatics, School of Medicine, Acibadem University, Atasehir, 34752 İstanbul, Turkey.
  • Gozuacik D From the Molecular Biology, Genetics and Bioengineering Program, Sabanci University, Orhanli-Tuzla, 34956 Istanbul, Turkey, dgozuacik@sabanciuniv.edu.
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  • 2016-06-22
Published in:
  • The Journal of biological chemistry. - 2016
ATG12-5-16
ATG5
RACK1
autophagy
lysosome
mammalian target of rapamycin (mTOR)
p70S6K
protein-protein interaction
signaling
Animals
Autophagy
Autophagy-Related Protein 12
Autophagy-Related Protein 5
Autophagy-Related Proteins
GTP-Binding Proteins
HEK293 Cells
Humans
Mice
Neoplasm Proteins
Protein Binding
Receptors for Activated C Kinase
Receptors, Cell Surface
English 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.
Language
  • English
Open access status
bronze
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Persistent URL
https://sonar.ch/global/documents/189567
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