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

Citation
Om. Martinez-estrada et al., Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial Caco-2 cells, J BIOL CHEM, 276(12), 2001, pp. 9291-9296
Citations number
22
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
0021-9258 → ACNP
Volume
276
Issue
12
Year of publication
2001
Pages
9291 - 9296
Database
ISI
SICI code
0021-9258(20010323)276:12<9291:AOJAMW>2.0.ZU;2-N
Abstract
We report here that junctional adhesion molecule (JAM) interacts with calci um/calmodulin-dependent serine protein kinase (CASK), a protein related to membrane-associated guanylate kinases. In Caco-2 cells, JAM and CASK were c oprecipitated and found to colocalize at intercellular contacts along the l ateral surface of the plasma membrane. Association of JAM with CASK require s the PSD95/dlg/ZO-1 (PDZ) domain of CASK and the putative PDZ-binding moti f Phe-Leu-Val(COOH) in the cytoplasmic tail of JAM. Temporal dissociation i n the junctional localization of the two proteins suggests that the associa tion with CASK is not required for recruiting JAM to intercellular junction s. Compared with mature intercellular contacts, junction assembly was chara cterized by both enhanced solubility of CASK in Triton X-100 and reduced am ounts of Triton-insoluble JAM-CASK complexes. We propose that JAM associati on with CASK is modulated during junction assembly, when CASK is partially released from its cytoskeletal associations.