Abstract
Synthetic peptides derived from transmembrane segments of G protein-coupled receptors (GPCR) are used to disrupt GPCR dimer interface. This peptide competition technique is an effective approach to map the dimer interface of GPCR and its functional significance. Here we present a technique to deliver synthetic transmembrane peptides to living mouse rod photoreceptors to disrupt rhodopsin (a prototypical member of Class A GPCRs) dimer formation in the endoplasmic reticulum (ER). We have shown that rhodopsin helix H1- or H8-peptide caused mislocalization of rhodopsin to the perinuclear endoplasmic reticulum (ER).
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