Related Experiment Video

Updated: Mar 7, 2026

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
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Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

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

Pornpun Aramsangtienchai1, Nicole A Spiegelman1, Ji Cao1

  • 1From the Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853.

The Journal of Biological Chemistry
|February 16, 2017
PubMed

Insights

Junctional adhesion molecule C (JAM-C) protein palmitoylation by DHHC7 regulates its tight junction localization and inhibits lung cancer cell migration. This finding offers a potential therapeutic target for controlling cancer metastasis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Junctional adhesion molecule C (JAM-C) is an immunoglobulin superfamily protein found in epithelial cells, endothelial cells, and leukocytes.
  • JAM-C plays roles in leukocyte migration, angiogenesis, cell adhesion, polarity, spermatogenesis, and metastasis.

Purpose of the Study:

  • To investigate the post-translational modification of JAM-C, specifically S-palmitoylation.
  • To identify the enzyme responsible for JAM-C palmitoylation and elucidate its functional consequences.

Main Methods:

  • Screening of all known palmitoyltransferases (DHHCs) to identify the JAM-C palmitoylating enzyme.
  • Ectopic expression and knockdown of DHHC7 to assess its effect on JAM-C palmitoylation.
  • Analysis of JAM-C localization to tight junctions and its role in A549 lung cancer cell migration using transwell assays.

Main Results:

  • JAM-C undergoes S-palmitoylation on juxtamembrane cysteine residues (Cys-264 and Cys-265).
  • DHHC7 was identified as the specific enzyme responsible for JAM-C palmitoylation.
  • DHHC7 activity enhances JAM-C S-palmitoylation, while DHHC7 knockdown reduces it.
  • Palmitoylation of JAM-C promotes its localization to tight junctions and inhibits the migration of A549 lung cancer cells.

Conclusions:

  • S-palmitoylation is a critical regulatory modification for JAM-C.
  • DHHC7-mediated palmitoylation of JAM-C influences its subcellular localization and function.
  • Targeting JAM-C S-palmitoylation presents a potential strategy for inhibiting cancer metastasis.

Keywords:
cell adhesioncell migrationchemical biologypost-translational modification (PTM)protein palmitoylationprotein-lipid interactiontight junction

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