Proximity measurements between H-2 antigens and the insulin receptor by fluorescence energy transfer: Evidence that a close association does not influence insulin binding

T. Liegler, J. Szollosi, W. Hyun, R. S. Goodenow

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Reports based on coprecipitation experiments have suggested that major histocompatibility complex class I products are complexed with the insulin receptor on the cell surface. Using an independent method that avoids the creation of immunoprecipitation artifacts during membrane solubilization, we have studied insulin receptor-class I product associations by determining the proximity between these class I products and the insulin receptor on intact cells with the use of fluorescence energy transfer. Significant energy transfer was seen between the insulin receptor and both murine H-2K- as well as H-2D-end products, indicating close proximity (e.g., within 10 nm). This cell-surface association is not from the relatively high class I density in that no significant energy transfer was measured between H-2K- vs. H-2D-end proteins. To extend these observations, we also tested whether class I products influence insulin-receptor binding and postbinding events as a result of their physical association. Using related cell lines positive and negative for class I expression, we found no correlation between insulin-receptor density or binding affinity with H-2 product expression. The class I-null variant, however, demonstrated an increase in insulin-mediated insulin-receptor internalization to suggest that if major histocompatibility complex class I products directly affect insulin-receptor function through specific cell-surface interactions, they may do so after ligand binding.

Original languageEnglish
Pages (from-to)6755-6759
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number15
DOIs
Publication statusPublished - 1991

Keywords

  • flow cytometry
  • internalization
  • major histocompatibility complex

ASJC Scopus subject areas

  • General

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