Snapin interacts with G-protein coupled receptor PKR2

Biochem Biophys Res Commun. 2016 Jan 15;469(3):501-6. doi: 10.1016/j.bbrc.2015.12.023. Epub 2015 Dec 11.

Abstract

Mutations in Prokineticin receptor 2 (PKR2), a G-protein-coupled receptor, have been identified in patients with Kallmann syndrome and/or idiopathic hypogonadotropic hypogonadism, characterized by delayed puberty and infertility. In this study, we performed yeast two-hybrid screening by using PKR2 C-terminus (amino acids 333-384) as a bait, and identified Snapin as a novel interaction partner for PKR2. The interaction of Snapin and PKR2 was confirmed in GST pull-down and co-immunoprecipitation studies. We further demonstrated that two α-helix domains in Snapin are required for the interaction. And the interactive motifs of PKR2 were mapped to YFK (343-345) and HWR (351-353), which shared a similar sequence of two aromatic amino acids followed by a basic amino acid. Disruption of Snapin-PKR2 interaction did not affect PKR2 signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2.

Keywords: G-protein coupled receptor; PKR2; Snapin; Yeast two hybrid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • HEK293 Cells
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Interaction Mapping
  • Receptors, G-Protein-Coupled / chemistry*
  • Receptors, G-Protein-Coupled / metabolism*
  • Receptors, Peptide / chemistry*
  • Receptors, Peptide / metabolism*
  • Vesicular Transport Proteins / chemistry*
  • Vesicular Transport Proteins / metabolism*

Substances

  • PROKR2 protein, human
  • Receptors, G-Protein-Coupled
  • Receptors, Peptide
  • SNAPIN protein, human
  • Vesicular Transport Proteins