Abstract
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Highlights
G protein-coupled receptors (GPCRs) are a family of proteins containing seven transmembrane helices that are crucial for cell signaling (Rosenbaum et al, 2009)
We further demonstrate that topology of CCR5 (CC chemokine receptor type 5), one of the GPCRs containing this motif, is inverted through Regulated Alternative Translocation (RAT) in lipopolysaccharides (LPS)-stimulated macrophages
After counting ~20 macrophages cultured in either condition, we found that the vast majority of CCR5 labeled by gold clusters had its N-terminus at the extracellular and intracellular side of plasma membranes, respectively, in cells cultured in the absence and presence of LPS (Figure 3L)
Summary
G protein-coupled receptors (GPCRs) are a family of proteins containing seven transmembrane helices that are crucial for cell signaling (Rosenbaum et al, 2009). This process depends on the GXXXN motif, as destruction of the motif locked the protein into the inverted topology regardless of ceramide treatments (Chen et al, 2016). These results suggest that functions of GPCRs may be regulated by topological inversion through RAT
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