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Internalisation of the protease-activated receptor 1: role of the third intracellular loop and of the cytoplasmic tail.

Abstract：

:To analyse the mechanisms of PAR-1 internalisation, we constructed several PAR-1 mutants and stably expressed them in CHO cells. Our study shows that the Ser(306)-->Ala mutation (S306A), which eliminates a potential site of phosphorylation by PKC in the third intracellular loop of PAR-1, did not change the rate of phosphorylation but reduced the rate of thrombin-induced internalisation of the PAR-1 mutant (58 versus 78% of membrane PAR-1 in 15 min, p<0.005). Deletion of the last 43 amino acid residues of the PAR-1 cytoplasmic tail completely suppressed the thrombin phosphorylation of the mutated receptor and significantly reduced its internalisation upon activation. This deletion also inhibited the PMA-induced and the agonist-independent internalisation of the receptor. The Tyr(371)--> Ala mutation (Y371A), in a NPXXY motif of the seventh transmembrane domain of the receptor had no effect on the receptor behaviour. Our results indicate that both the C-tail and the third intracellular loop are involved in PAR-1 internalisation induced by thrombin while only the C-tail plays a role in the PMA-induced and in the agonist-independent PAR-1 internalisation.

journal_name

Int J Mol Med

journal_title

International journal of molecular medicine

authors

Chen X,Berrou J,Vigneau C,Delarue F,Rondeau E

doi

10.3892/ijmm.7.6.653

subject

Has Abstract

pub_date

2001-06-01 00:00:00

pages

653-8

issue

6

eissn

1107-3756

issn

1791-244X

journal_volume

7

pub_type

杂志文章

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