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The palmitoylation state of PMP22 modulates epithelial cell morphology and migration

Susie J Zoltewicz1, Sooyeon Lee, Vinita G Chittoor

  • 1Department of Neuroscience, College of Medicine, McKnight Brain Institute, University of Florida, Gainesville, FL 32610, USA.

ASN Neuro
|November 7, 2012
PubMed

Insights

Palmitoylation of peripheral myelin protein 22 (PMP22) at cysteine 85 is crucial. Blocking this modification alters epithelial cell shape and motility, impacting cell migration.

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • Peripheral myelin protein 22 (PMP22) is a key component of peripheral nerve myelin and epithelial intercellular junctions.
  • The post-translational modifications of PMP22, particularly palmitoylation, are not well understood.

Purpose of the Study:

  • To investigate the role of palmitoylation at cysteine 85 (C85) in PMP22 function.
  • To determine the impact of PMP22 palmitoylation on epithelial cell behavior, including cell shape and migration.

Main Methods:

  • Computational prediction of PMP22 palmitoylation sites using CSS-Palm 2.0 software.
  • Site-directed mutagenesis of C85 to serine (C85S) to create non-palmitoylated PMP22.
  • Stable expression of wild-type (WT) and C85S-PMP22 in Schwann and MDCK cells.
  • Monitoring palmitoylation using 17-octadecynoic acid (17-ODYA).
  • Assessing cell morphology and migration using wound-healing assays.

Main Results:

  • Mutation of C85 successfully blocked PMP22 palmitoylation in both Schwann and MDCK cells.
  • Overexpression of non-palmitoylated C85S-PMP22 induced significant cell spreading and monolayer thinning.
  • While WT-PMP22 expressing cells showed resistance to migration, C85S-PMP22 expressing cells exhibited lamellipodial protrusions and migrated similarly to controls.

Conclusions:

  • Palmitoylation of PMP22 at C85 is essential for regulating epithelial cell shape.
  • The palmitoylation status of PMP22 critically influences epithelial cell motility and migration.

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