2. Academic Validation
  3. S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight Junction Localization and Cell Migration

S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight Junction Localization and Cell Migration

  • J Biol Chem. 2017 Mar 31;292(13):5325-5334. doi: 10.1074/jbc.M116.730523.
Pornpun Aramsangtienchai 1,  Nicole A Spiegelman 1,  Ji Cao 1,  Hening Lin 2
Affiliations

Affiliations

  • 1 From the Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853.
  • 2 From the Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853 hl379@cornell.edu.
PMID: 28196865 DOI: 10.1074/jbc.M116.730523
Abstract

Junctional adhesion molecule C (JAM-C) is an immunoglobulin superfamily protein expressed in epithelial cells, endothelial cells, and leukocytes. JAM-C has been implicated in leukocyte transendothelial migration, angiogenesis, cell adhesion, cell polarity, spermatogenesis, and metastasis. Here, we show that JAM-C undergoes S-palmitoylation on two juxtamembrane cysteine residues, Cys-264 and Cys-265. We have identified DHHC7 as a JAM-C palmitoylating Enzyme by screening all known palmitoyltransferases (DHHCs). Ectopic expression of DHHC7, but not a DHHC7 catalytic mutant, enhances JAM-C S-palmitoylation. Moreover, DHHC7 knockdown decreases the S-palmitoylation level of JAM-C. Palmitoylation of JAM-C promotes its localization to tight junctions and inhibits transwell migration of A549 lung Cancer cells. These results suggest that S-palmitoylation of JAM-C can be potentially targeted to control Cancer metastasis.

Keywords

cell adhesion; cell migration; chemical biology; post-translational modification (PTM); protein palmitoylation; protein-lipid interaction; tight junction.

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