Metabotropic glutamate receptor 5 is a disulfide-linked dimer

Carmelo Romano, Wan Lin Yang, Karen L. O'Malley

Research output: Contribution to journalArticlepeer-review

438 Scopus citations

Abstract

The sequences of the metabotropic glutamate receptors (mGluRs) show little homology with other members of the G protein-coupled receptor family and exhibit several distinctive features, including a large N-terminal extracellular domain with 17 cysteines in conserved positions. Here we demonstrate that mGluR5, as well as other mGluRs, behave as species approximately twice as large as expected from their sequence, but reducing conditions cause a decrease to the predicted molecular mass. Co- immunoprecipitation experiments using wild type and epitope-tagged receptors demonstrate that this is due to specific, disulfide-dependent dimerization of the receptor. The intermolecular disulfide that mediates dimerization occurs in the extracellular domain, within about 17 kDa from the N terminus.

Original languageEnglish
Pages (from-to)28612-28616
Number of pages5
JournalJournal of Biological Chemistry
Volume271
Issue number45
DOIs
StatePublished - 1996

Fingerprint

Dive into the research topics of 'Metabotropic glutamate receptor 5 is a disulfide-linked dimer'. Together they form a unique fingerprint.

Cite this