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Cell surface expression of the melanocortin-4 receptor is dependent on a C-terminal di-isoleucine sequence at codons

Donald VanLeeuwen1, Michael E Steffey, Christopher Donahue

  • 1Pfizer Global Research and Development, Ann Arbor, MI 48105, USA.

Insights

Mutations in the melanocortin-4 receptor (MC4R) C-terminus, specifically at isoleucine residues 316/317, impair receptor function and cell surface expression, contributing to obesity. These findings highlight the importance of this motif for MC4R activity.

Area of Science:

  • Genetics
  • Molecular Biology
  • Endocrinology

Background:

  • Loss-of-function mutations in the human melanocortin-4 receptor (MC4R) are a significant genetic cause of obesity.
  • A C-terminal di-isoleucine motif (residues 316/317) is crucial for MC4R cell surface targeting and function.

Purpose of the Study:

  • To investigate the functional consequences of a specific MC4R mutation (I317T) found in an obese individual.
  • To examine the role of the C-terminal di-isoleucine motif in MC4R cell surface expression and function.

Main Methods:

  • Oligonucleotide-directed mutagenesis was used to create single (I316T, I317T) and double (I316T,I317T) MC4R mutants.
  • Receptor function was assessed by measuring cAMP accumulation in response to NDP-alpha-MSH or forskolin.
  • Cell surface expression was quantified using radioligand binding, immunocytochemistry, and flow cytometry.

Main Results:

  • Single MC4R mutants (I316T, I317T) showed a 40% reduction in maximal cAMP generation compared to wild-type.
  • The double mutant (I316T,I317T) further decreased function to 40% of control levels.
  • Reduced receptor function correlated with decreased cell surface expression, while transcript levels remained unaffected.

Conclusions:

  • The C-terminal di-isoleucine motif is critical for MC4R cell surface expression.
  • Mutations affecting residues 316 or 317 of MC4R are predicted to cause MC4R hypofunction, potentially leading to obesity.

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