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- W2046409929 abstract "About 5–10% of the G protein-coupled receptors (GPCRs) contain N-terminal signal peptides that are cleaved off by the signal peptidases of the endoplasmic reticulum (ER) during the translocon-mediated receptor insertion into the ER membrane. The reason as to why only a subset of the GPCRs requires these additional signal peptides was addressed in the past decade only by a limited number of studies. Recent progress suggests that signal peptides of GPCRs do not only serve the classical ER targeting and translocon gating functions as described for the signal peptides of secretory proteins. In the case of GPCRs, uncleaved pseudo signal peptides may regulate receptor expression at the plasma membrane and may also influence G protein coupling. Moreover, signal peptides of GPCRs seem to match functionally with sequences of the mature N tails. In this review, we summarize the current knowledge about cleavable signal peptides of GPCRs and address the question whether these sequences may be future drug targets in pharmacology." @default.
- W2046409929 created "2016-06-24" @default.
- W2046409929 creator A5020668359 @default.
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- W2046409929 date "2012-04-01" @default.
- W2046409929 modified "2023-10-17" @default.
- W2046409929 title "Functional significance of cleavable signal peptides of G protein-coupled receptors" @default.
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- W2046409929 doi "https://doi.org/10.1016/j.ejcb.2011.02.006" @default.
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