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PICK‐1: A scaffold protein that interacts with Nectins and JAMs at cell junctions
Author(s) -
Reymond Nicolas,
Garrido-Urbani Sarah,
Borg Jean-Paul,
Dubreuil Patrice,
Lopez Marc
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.010
Subject(s) - jams , scaffold protein , scaffold , microbiology and biotechnology , chemistry , biophysics , biology , computer science , signal transduction , food science , database
Nectin adhesion molecules are involved in the early steps of cell junction formation. Later during the polarisation process, Nectins are components of epithelial adherens junctions where they are indirectly associated with the E‐cadherin/Catenins complex via the adaptator AF‐6. To have a better understanding of Nectin‐based cell junctions, we looked for some new Nectins’ partners. We demonstrate that the scaffold molecule PICK‐1, involved in the clustering of junctional receptors in synaptic junctions, interacts directly with Nectins in a PSD‐95/Dlg/ZO‐1 domain‐dependent manner and is localised at adherens junctions in epithelial cells. Finally, we observed that protein interacting with C‐kinase‐1 (PICK‐1) also interacts directly with the junctional adhesion molecules, and we suggest that PICK‐1 could be involved in the regulation of both adherens and tight junctions in epithelial cells.