Characterisation of the adiponectin receptors: the non-conserved N-terminal region of AdipoR2 prevents its expression at the cell-surface

Biochem Biophys Res Commun. 2013 Mar 1;432(1):28-33. doi: 10.1016/j.bbrc.2013.01.092. Epub 2013 Jan 31.

Abstract

Adiponectin is a beneficial adipokine with insulin-sensitizing, anti-inflammatory and anti-atherogenic effects. These effects are mediated by two poorly characterised, closely related, atypical seven-transmembrane receptors. In the current report we have used C-terminal, epitope-tagged AdipoR1 and AdipoR2 constructs to monitor cell-surface expression by indirect immunofluorescence microscopy and quantitative plate-based analysis. We demonstrate that only AdipoR1 is constitutively expressed on the cell-surface. Further investigations, involving characterisation of a number of chimeric and truncated constructs, show the non-conserved region of AdipoR2 (residues 1-81) restricts its cell-surface expression. Introduction or deletion of this region, into AdipoR1 or AdipoR2, resulted in inhibition or promotion of cell-surface expression, respectively. We also confirmed that AdipoR1 and AdipoR2 can form heterodimers when co-expressed and that co-expression leads to the cell-surface expression of AdipoR2. Collectively these studies demonstrate that the non-conserved region of AdipoR2 restricts its cell-surface expression and raise the possibility that the majority of cell-surface AdipoR2 may be present in the form of heterodimers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Cell Membrane / metabolism*
  • Cricetinae
  • Humans
  • Molecular Sequence Data
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Receptors, Adiponectin / genetics
  • Receptors, Adiponectin / metabolism*
  • Recombinant Fusion Proteins / metabolism

Substances

  • ADIPOR1 protein, human
  • ADIPOR2 protein, human
  • Receptors, Adiponectin
  • Recombinant Fusion Proteins