Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells

J Biol Chem. 2001 Mar 23;276(12):9291-6. doi: 10.1074/jbc.M006991200. Epub 2000 Dec 18.


We report here that junctional adhesion molecule (JAM) interacts with calcium/calmodulin-dependent serine protein kinase (CASK), a protein related to membrane-associated guanylate kinases. In Caco-2 cells, JAM and CASK were coprecipitated and found to colocalize at intercellular contacts along the lateral surface of the plasma membrane. Association of JAM with CASK requires the PSD95/dlg/ZO-1 (PDZ) domain of CASK and the putative PDZ-binding motif Phe-Leu-Val(COOH) in the cytoplasmic tail of JAM. Temporal dissociation in the junctional localization of the two proteins suggests that the association with CASK is not required for recruiting JAM to intercellular junctions. Compared with mature intercellular contacts, junction assembly was characterized by both enhanced solubility of CASK in Triton X-100 and reduced amounts of Triton-insoluble JAM-CASK complexes. We propose that JAM association with CASK is modulated during junction assembly, when CASK is partially released from its cytoskeletal associations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Caco-2 Cells
  • Calcium-Calmodulin-Dependent Protein Kinases*
  • Cell Adhesion Molecules / metabolism*
  • Cytoplasm / enzymology
  • DNA Primers
  • Guanylate Kinases
  • Humans
  • Junctional Adhesion Molecules
  • Nucleoside-Phosphate Kinase / metabolism*
  • Protein Binding
  • Subcellular Fractions / enzymology


  • Cell Adhesion Molecules
  • DNA Primers
  • Junctional Adhesion Molecules
  • CASK kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Nucleoside-Phosphate Kinase
  • Guanylate Kinases