Related Experiment Video
Updated: May 23, 2025

Study of Protein-protein Interactions in Autophagy Research
Published on: September 9, 2017
Conserved regulation of autophagosome-lysosome fusion through YKT6 phosphorylation
Pablo Sánchez-Martín1, Claudine Kraft1,2
1Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Abstract:
YKT6 is a SNARE (Soluble N-ethylmaleimide-Sensitive Fusion Protein Attachment Protein Receptor) protein governing membrane fusion events of several cellular organelles. In autophagy, YKT6 is involved in early phagophore formation as well as directly in the fusion process between autophagosomes and the lytic compartment. Recently we showed in yeast, mammalian cells, and nematodes that the function of YKT6 in autophagy can be regulated by phosphorylation. Atg1/ULK1 (Unc-51-like kinase 1)-dependent phosphorylation of YKT6 results in autophagy defects during both early (autophagosome formation) and late (autophagosome-lysosome fusion) steps, ultimately resulting in decreased survival of mammalian cells due to defective stress-induced autophagy. These findings show that not only the function but also the regulation of YKT6 is conserved across species.
Related Concept Videos
Autophagy
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
Delivery Pathways to the Lysosome
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Autophagic Cell Death
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
PI3K/mTOR/AKT Signaling Pathway
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....

