L-type prostaglandin D synthase regulates the trafficking of the PGD₂ DP1 receptor by interacting with the GTPase Rab4.

ABSTRACT: Accumulating evidence indicates that G protein-coupled receptors (GPCRs) interact with Rab GTPases during their intracellular trafficking. How GPCRs recruit and activate the Rabs is unclear. Here, we report that depletion of endogenous L-type prostaglandin D synthase (L-PGDS) in HeLa cells inhibited recycling of the prostaglandin D₂ (PGD₂) DP1 receptor (DP1) to the cell surface after agonist-induced internalization and that L-PGDS overexpression had the opposite effect. Depletion of endogenous Rab4 prevented l-PGDS-mediated recycling of DP1, and l-PGDS depletion inhibited Rab4-dependent recycling of DP1, indicating that both proteins are mutually involved in this pathway. DP1 stimulation promoted its interaction through its intracellular C terminus with Rab4, which wa

SUBMITTER: Binda C 

PROVIDER: S-EPMC6851311 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature