text: Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation | Journal of Cell Science
  Cortactin is a scaffolding platform for the E-Cadherin adhesion complex controlled by protein kinase D1 phosphorylation
  J Cell Sci 2016 : jcs.184721 doi: 10.1242/jcs.184721 Published 13 May 2016
  Department of Cellular and Molecular Medicine, Katholieke Universiteit Leuven, Campus Gasthuisberg O/N1 - Herestraat 49 bus 901, 3000 Leuven (Belgium)
  Department for Animal Breeding and Biotechnology, LMU Munich, Gene Center, Feodor-Lynen- Str. 25, D-81377 Munich, Germany
  Department of Visceral Surgery, Ulm University, Albert-Einstein-Allee 23, D-89081 Ulm, Germany
  Dynamic regulation of cell-cell adhesion by the coordinated formation and dissolution of E–Cadherin-based adherens junctions (AJs) is critical for tissue homeostasis. The actin-binding protein Cortactin interacts with E-Cadherin and enables F-actin accumulation at AJs. We here were interested to study broader functional interactions of Cortactin in adhesion complexes. In line with literature, we demonstrate that Cortactin binds to E-Cadherin and a posttranslational modification of Cortactin, RhoA–induced phosphorylation by PKD1 at S298, impairs AJ assembly and supports their dissolution. Two novel S298-phosphorylation-dependent interactions were identified: Phosphorylation of Cortactin decreases its interaction with beta-Catenin and the actin-binding protein Vinculin. Secondly, binding of Vinculin to beta-Catenin as well as linkage of Vinculin to F-actin are also significantly compromised. Accordingly, we found that regulation of cell-cell adhesion by phosphorylation of Cortactin downstream of RhoA/PKD1 is vitally dependent on Vinculin–mediated protein interactions. Thus, Cortactin unexpectedly is an important integration node for the dynamic regulation of protein complexes during breakdown and formation of AJs.
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