The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression.
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Zampatis DE, Rutz C, Furkert J, Schmidt A, Wustenhagen D, Kubick S, Tsopanoglou NE, Schulein R
The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression.
FEBS Lett. 2012 Jul 30;586(16):2351-9. doi: 10.1016/j.febslet.2012.05.042. Epub 2012 May 31.
- PubMed ID
- 22659187 [ View in PubMed]
- 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 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.