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Chaperone mediated autophagy inhibitor12/9/2023 ![]() ![]() (D) Percentage of p-PLIN2 relative to total PLIN2 levels in the same cells as in (B). Values are expressed relative to total levels of PLIN2 in control cells that was given an arbitrary value of 1. (C) Levels of total, phosphorylated and unphosphorylated PLIN2 in the same cells as in (B). ACTB/β-actin was used as loading control. (B) Total cell lysates from CTR and L2A − cells treated with OL and incubated with regular medium (RM) after OL treatment. Top shows immunoblot for PLIN2 without Phos-tag. (A) Total cell lysates from cells cultured with or without OL were subjected to Phos-tag gel electrophoresis and immunoblotted for PLIN2. Our results highlight a role for posttranslational modifications in priming proteins to be amenable for degradation by CMA.Ĭhaperones lipid droplets lysosome-associated membrane protein 2A lysosomes perilipins protein degradation. Here, we report that phosphorylation of PLIN2 is dependent on AMPK and occurs after the interaction of PLIN2 with the CMA chaperone HSPA8/Hsc70. PLIN2 phosphorylation was observed upon induction of lipolysis, but the phosphorylating kinase and the relation of this phosphorylation with CMA of PLIN2 remained unknown. CMA selectively degrades the lipid droplet proteins perilipins (PLIN) 2 and 3 from the lipid droplet surface, thus, facilitating the recruitment of cytosolic lipases and autophagy effector proteins to the lipid droplets. We recently demonstrated that chaperone-mediated autophagy (CMA) is required for the initiation of lipolysis by either of these independent lipolytic pathways. Lipids stored in lipid droplets are hydrolyzed via either cytosolic lipases or a selective form of macroautophagy known as lipophagy.
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