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Figure: A lysosomal is an acidic intracellular organelle that is essential
for the degradation of various cellular components.
When lysosomal membranes are damaged, lysosomal hydrolases are released into the cytoplasm, causing a stress response or cell death
.
Here, we show that a newly discovered protein complex can recognize damaged lysosomes and ubiquitinate the substrate LAMP2
.
This recognition induces selective autophagy
.
Autophagy is a self-degrading process
that cells use to remove unwanted or damaged components.
In a recent report published in Cells in the United States, the team described a process called lysosomes, a specific form of selective autophagy responsible for clearing damaged lysosomes
.
"We know from previous studies that lysosomes can be labeled by a specific enzyme, SCFFBXO27 through a process called polygenization," said Teranishi Hirofumi, one of the study's lead authors
.
The team used polystyrene beads coated with a reagent, which can induce endosomal damage and then be ubiquitinated
.
"With the help of molecular techniques, we can inhibit the expression of these different proteins, and we found that proteins known as CUL4A, DDB1, and WDFY1 form a complex that responds to lysosomal damage,"
explains Maho Hamasaki, senior author of the study.
Further characterization shows that this complex plays a priority role in the lysozyme process and promotes the addition
of ubiquitin molecules.
Teranishi said: "We want to know which part of the lysosomes is recognized
by this protein complex.
The team also found that the presence of LAMP2 and its interaction with WDFY1 is critical
to initiating the bacteriolytic process.
essay
Identification of CUL4A- DDB1-WDFY1 as the E3 ubiquitin ligase complex to initiate lysophagy
