Evidence for leptin receptor isoforms heteromerization at the cell surface

FEBS Lett. 2010 Jun 3;584(11):2213-7. doi: 10.1016/j.febslet.2010.03.033. Epub 2010 Mar 27.

Abstract

Leptin mediates its metabolic effects through several leptin receptor (LEP-R) isoforms. In humans, long (LEPRb) and short (LEPRa,c,d) isoforms are generated by alternative splicing. Most of leptin's effects are believed to be mediated by the OB-Rb isoform. However, the role of short LEPR isoforms and the possible existence of heteromers between different isoforms are poorly understood. Using BRET1 and optimized co-immunoprecipitation, we observed LEPRa/b and LEPRb/c heteromers located at the plasma membrane and stabilized by leptin. Given the widespread coexpression of LEPRa and LEPRb, our results suggest that LEPRa/b heteromers may represent a major receptor species in most tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / metabolism
  • Cell Membrane / metabolism*
  • Cells / metabolism
  • Humans
  • Immunoprecipitation
  • Leptin / metabolism
  • Protein Isoforms / metabolism
  • Receptors, Leptin*

Substances

  • Carrier Proteins
  • Leptin
  • Protein Isoforms
  • Receptors, Leptin