α -catenin phosphorylation is elevated during mitosis to resist apical rounding and epithelial barrier leak.

ABSTRACT: Epithelial cell cohesion and barrier function critically depend on α -catenin, an actin-binding protein and essential constituent of cadherin-catenin-based adherens junctions. α -catenin undergoes actomyosin force-dependent unfolding of both actin-binding and middle domains to strongly engage actin filaments and its various effectors, where this mechanosensitivity is critical for adherens junction function. We previously showed that α -catenin is highly phosphorylated in an unstructured region that links mechanosensitive middle- and actin-binding domains (known as the P-linker region), but the cellular processes that promote α -catenin phosphorylation have remained elusive. Here, we leverage a previously published phosphor-proteomic data set to show that the α -catenin P-linker region is m

SUBMITTER: Le PM 

PROVIDER: S-EPMC11398478 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature