LPA1-mediated inhibition of CXCR4 attenuates CXCL12-induced signaling and cell migration.

ABSTRACT:

Background

G protein-coupled receptor heteromerization is believed to exert dynamic regulatory impact on signal transduction. CXC chemokine receptor 4 (CXCR4) and its ligand CXCL12, both of which are overexpressed in many cancers, play a pivotal role in metastasis. Likewise, lysophosphatidic acid receptor 1 (LPA₁) is implicated in cancer cell proliferation and migration. In our preliminary study, we identified LPA₁ as a prospective CXCR4 interactor. In the present study, we investigated in detail the formation of the CXCR4-LPA₁ heteromer and characterized the unique molecular features and function of this heteromer.

Methods

We employed bimolecular fluorescence complementation, bioluminescence resonance energy transfer, and proximity ligation

SUBMITTER: Hong JM 

PROVIDER: S-EPMC10518940 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature