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The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression

Item Type:Article
Title:The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression
Creators Name:Zampatis, D.E. and Rutz, C. and Furkert, J. and Schmidt, A. and Wuestenhagen, D. and Kubick, S. and Tsopanoglou, N.E. and Schuelein, R.
Abstract:The protease-activated receptor 1 (PAR1) is activated by thrombin cleavage releasing the physiologically-relevant parstatin peptide (residues 1-41). However, the actual length of parstatin was unclear since the receptor may also possess a cleavable signal peptide (residues 1-21) according to prediction programs. Here, we show that this putative signal peptide is indeed functional and removed from the PAR1 resolving the question of parstatin length. Moreover, we show that deletion of the sequence encoding the signal peptide may surprisingly play a role in stabilization of the PAR1 mRNA, a function which would be novel for a G protein-coupled receptor.
Keywords:PAR1, Signal Peptide, mRNA Stability, G Protein-Coupled Receptor
Source:FEBS Letters
ISSN:0014-5793
Publisher:Elsevier (The Netherlands)
Volume:586
Number:16
Page Range:2351-2359
Date:31 May 2012
Official Publication:https://doi.org/10.1016/j.febslet.2012.05.042
PubMed:View item in PubMed

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