Calcium binding protects E-cadherin from cleavage by Helicobacter pylori HtrA.

ABSTRACT:

Background

The cell adhesion and tumor suppressor protein E-cadherin is an important factor in the establishment and maintenance of epithelial integrity. E-cadherin is a single transmembrane protein, which consists of an intracellular domain (IC), a transmembrane domain (TD), and five extracellular domains (EC). EC domains form homophilic interactions in cis and trans that require calcium binding to the linker region between the EC domains. In our previous studies, we identified the serine protease high temperature requirement A (HtrA) from the human pathogen and class-I carcinogen Helicobacter pylori (H. pylori) as a bacterial E-cadherin-cleaving protease that targets the linker region of the EC domains, thereby disrupting gastric epithelial integrity. However, it remains unclear

SUBMITTER: Schmidt TP 

PROVIDER: S-EPMC4895972 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature