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LDO proteins and Vac8 form a vacuole-lipid droplet contact site required for lipophagy in response to starvation

LDO proteins and Vac8 form a vacuole-lipid droplet contact site required for lipophagy in response to starvation

FromPaperPlayer biorxiv cell biology


LDO proteins and Vac8 form a vacuole-lipid droplet contact site required for lipophagy in response to starvation

FromPaperPlayer biorxiv cell biology

ratings:
Length:
20 minutes
Released:
Apr 21, 2023
Format:
Podcast episode

Description

Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.04.21.537797v1?rss=1

Authors: Alvarez-Guerra, I., Block, E., Broeskamp, F., Gabrijelcic, S., de Ory, A., Habernig, L., Andreasson, C., Levine, T., Höög, J. L., Büttner, S.

Abstract:
Lipid droplets (LDs) are fat storage organelles critical for energy and lipid metabolism. Upon nutrient exhaustion, cells consume LDs via gradual lipolysis or via lipophagy, the en bloc uptake of LDs into the vacuole. Here, we show that LDs dock to the vacuolar membrane via a contact site that is required for lipophagy in yeast. The LD-localized LDO proteins carry an intrinsically disordered region that associates with vacuolar Vac8 to form vCLIP, the vacuolar-LD contact site. Nutrient limitation drives vCLIP formation, and its inactivation blocks lipophagy. Vac8 is sufficient to recruit LDs to cellular membranes. We establish a functional link between lipophagy and microautophagy of the nucleus, both requiring Vac8 to form respective contact sites upon metabolic stress. In sum, we unravel the molecular architecture of vCLIP, a contact site required for lipophagy, and find that Vac8 provides a platform for multiple and competing contact sites associated with autophagy.

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Podcast created by Paper Player, LLC
Released:
Apr 21, 2023
Format:
Podcast episode

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