AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA

Research output: Contribution to journalArticle

67 Scopus citations

Abstract

Lipids stored in lipid droplets are hydrolyzed via either cytosolic lipases or a selective form of macroautophagy known as lipophagy. We recently demonstrated that chaperone-mediated autophagy (CMA) is required for the initiation of lipolysis by either of these independent lipolytic pathways. 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. PLIN2 phosphorylation was observed upon induction of lipolysis, but the phosphorylating kinase and the relation of this phosphorylation with CMA of PLIN2 remained unknown. Here, we report that phosphorylation of PLIN2 is dependent on AMPK and occurs after the interaction of PLIN2 with the CMA chaperone HSPA8/Hsc70. Our results highlight a role for posttranslational modifications in priming proteins to be amenable for degradation by CMA.

Original languageEnglish (US)
Pages (from-to)432-438
Number of pages7
JournalAutophagy
Volume12
Issue number2
DOIs
StatePublished - Jan 1 2016

Keywords

  • Chaperones
  • Lipid droplets
  • Lysosome-associated membrane protein 2A
  • Lysosomes
  • Perilipins
  • Protein degradation

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA'. Together they form a unique fingerprint.

  • Cite this