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Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration

Narayanapanicker Anilkumar1, Takamasa Uekita, John R Couchman

  • 1Department of Matrix Biology, Kennedy Institute of Rheumatology Division, Imperial College London, London, UK.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|June 11, 2005
PubMed

Insights

Matrix metalloproteinase MT1-MMP

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Matrix metalloproteinase MT1-MMP is a type I transmembrane proteinase.
  • MT1-MMP plays a critical role in promoting cell migration and invasion.

Purpose of the Study:

  • To investigate the role of posttranslational modifications in MT1-MMP function.
  • To determine the impact of palmitoylation on MT1-MMP-mediated cell migration and internalization.

Main Methods:

  • Site-directed mutagenesis to create palmitoylation-defective MT1-MMP mutants (C574A).
  • Analysis of cell migration and invasion assays.
  • Investigating protein internalization pathways (clathrin-mediated and caveolae-mediated).

Main Results:

  • MT1-MMP undergoes palmitoylation at Cys574, which is essential for its cell migration-promoting activity.
  • Palmitoylation is critical for MT1-MMP's clathrin-mediated internalization.
  • A palmitoylation-defective mutant (C574A) showed impaired cell migration and altered internalization via caveolae.
  • The position of the palmitoylated cysteine relative to the LLY573 motif is crucial for MT1-MMP function.

Conclusions:

  • Palmitoylation of MT1-MMP at Cys574 is a key posttranslational modification regulating its role in cell migration.
  • This lipid modification dictates the internalization pathway and subsequent cellular functions of MT1-MMP.

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