Janus kinase 3 regulates adherens junctions and epithelial mesenchymal transition through β-catenin.

ABSTRACT: Compromise in adherens junctions (AJs) is associated with several chronic inflammatory diseases. We reported previously that Janus kinase 3, a non-receptor tyrosine kinase, plays a crucial role in AJ formation through its interaction with β-catenin. In this report, we characterize the structural determinants responsible for Jak3 interactions with β-catenin and determine the functional implications of previously unknown tyrosine residues on β-catenin phosphorylated by Jak3. We demonstrate that Jak3 autophosphorylation was the rate-limiting step during Jak3 trans-phosphorylation of β-catenin, where Jak3 directly phosphorylated three tyrosine residues, viz. Tyr³⁰, Tyr⁶⁴, and Tyr⁸⁶ in the N-terminal domain (NTD) of β-catenin. However, prior phosphorylati

SUBMITTER: Mishra J 

PROVIDER: S-EPMC5633104 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature