Journal
FEBS LETTERS
Volume 586, Issue 16, Pages 2351-2359Publisher
WILEY
DOI: 10.1016/j.febslet.2012.05.042
Keywords
PAR1; Signal peptide; mRNA stability; G protein-coupled receptor
Funding
- Deutsche Forschungsgemeinschaft [SFB 449]
- University of Patras
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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 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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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