DUSP3 regulates phosphorylation-mediated degradation of occludin and is required for maintaining epithelial tight junction.

ABSTRACT:

Background

Tight junctions (TJ) are multi-protein complexes that hold epithelial cells together and form structural and functional barriers for maintaining proper biological activities. Dual specificity phosphatase 3 (DUSP3), a suppressor of multiple protein tyrosine (Tyr) kinases, is decreased in lung cancer tissues. Here we demonstrated the role of DUSP3 in regulation of epithelial TJ.

Methods

Barrier functions of TJ were examined in wild-type or DUSP3-deficient lung epithelial cells. Animal and clinical data were analyzed for the association between DUSP3 deficiency and lung cancer progression. Proximity ligation assay, immunoblotting, and phosphatase assay were performed to study the effect of DUSP3 on the TJ protein occludin (OCLN). Mutations of Tyr residues on OCLN sho

SUBMITTER: Chou HC 

PROVIDER: S-EPMC9199239 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature