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.

Martinez Estrada, O., Villa, A., Breviario, F., Orsenigo, F., Dejana, E., Bazzoni, G. (2001). Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 276(12), 9291-9296 [10.1074/jbc.M006991200].

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

VILLA, ANTONELLO;
2001

Abstract

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.
Articolo in rivista - Articolo scientifico
Cell Adhesion Molecules; Nucleoside-Phosphate Kinase; Caco-2 Cells; DNA Primers; Base Sequence; Guanylate Kinase; Calcium-Calmodulin-Dependent Protein Kinases; Protein Binding; Subcellular Fractions; Humans; Cytoplasm
English
23-mar-2001
276
12
9291
9296
none
Martinez Estrada, O., Villa, A., Breviario, F., Orsenigo, F., Dejana, E., Bazzoni, G. (2001). Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 276(12), 9291-9296 [10.1074/jbc.M006991200].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/18662
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