The Tnfaip8-PE complex is a novel upstream effector in the anti-autophagic action of insulin

Sci Rep. 2017 Jul 24;7(1):6248. doi: 10.1038/s41598-017-06576-3.

Abstract

Defective hepatic autophagy is observed in obesity and diabetes, whereas autophagy is inhibited by insulin in hepatocytes. Insulin-induced anti-autophagy is mediated by non-canonical Gαi3 signaling via an unknown mechanism. Previously, we identified the anti-autophagic activity of Tnfaip8 via activation of mammalian target of rapamycin (mTOR) in the nervous system. Here, we demonstrate that insulin temporally induces Tnfaip8, which mediates the anti-autophagic action of insulin through formation of a novel ternary complex including Tnfaip8, phosphatidylethanolamine (PE) and Gαi3. Specifically, an X-ray crystallographic study of Tnfaip8 from Mus musculus (mTnfaip8) at 2.03 Å together with LC-MS analyses reveals PE in the hydrophobic cavity. However, an mTnfaip8 mutant lacking PE does not interact with Gαi3, indicating that the PE component is critical for the anti-autophagic action of mTnfaip8 via interaction with Gαi3. Therefore, the mTnfaip8-PE complex may act as an essential upstream effector via ternary complex formation most likely with active Gαi3 during insulin-induced anti-autophagy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis Regulatory Proteins / chemistry*
  • Apoptosis Regulatory Proteins / metabolism*
  • Autophagy*
  • Crystallography, X-Ray
  • GTP-Binding Protein alpha Subunits, Gi-Go / chemistry
  • GTP-Binding Protein alpha Subunits, Gi-Go / metabolism*
  • Insulin / metabolism*
  • Mice
  • Phosphatidylethanolamines / chemistry
  • Phosphatidylethanolamines / metabolism*
  • Protein Binding
  • Protein Conformation
  • Sequence Homology

Substances

  • Apoptosis Regulatory Proteins
  • Insulin
  • Phosphatidylethanolamines
  • TNFAIP8 protein, mouse
  • phosphatidylethanolamine
  • GTP-Binding Protein alpha Subunits, Gi-Go