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The SWR1 complex prevents the vacuolar delivery of ATG proteins through a noncanonical pathway
The SWR1 complex stops ATG proteins from being sent to the cell’s storage compartments by an unusual route
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Abstract
The SWR1 chromatin remodeling complex is identified as a critical regulator that prevents the vacuolar delivery of multiple autophagy proteins.
- Autophagy involves the formation of autophagosomes, which are structures that enclose cellular components for degradation.
- The mechanisms that prevent autophagy-related proteins from being degraded in the vacuole remain unclear in yeast.
- Genome-wide screening revealed that the SWR1 complex plays an essential role in regulating the fate of autophagy proteins.
- The function of the SWR1 complex is dependent on its structural integrity and ATPase activity.
- The interaction between the SWR1 subunit Rvb1 and Atg21 is crucial for the localization of SWR1 to the phagophore assembly site.
- Disruption of the Atg21-Rvb1 interaction leads to the accumulation of autophagy proteins in the vacuole.
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