@article{588b1580596211dd8d9f000ea68e967b,
title = "Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration.",
abstract = "MT1-MMP is a type I transmembrane proteinase that promotes cell migration and invasion. Here, we report that MT1-MMP is palmitoylated at Cys574 in the cytoplasmic domain, and this lipid modification is critical for its promotion of cell migration and clathrin-mediated internalization. The palmitoylation-defective mutant (C574A) failed to promote cell migration and was not internalized through clathrin pathway like wild-type, but it was internalized through the caveolae pathway. Reintroducing a cysteine at different positions in the cytoplasmic tail of the C574A mutant revealed that the position of the palmitoylated cysteine relative to LLY573, a motif that interacts with mu2 subunit of adaptor protein 2, is critical for the cell motility-promoting activity of MT1-MMP and its clathrin-mediated internalization. Taken together, palmitoylation of MT1-MMP is one of the key posttranslational modifications that determines MT1-MMP-dependent cell migration.",
author = "Narayanapanicker Anilkumar and Takamasa Uekita and Couchman, {John R} and Hideaki Nagase and Motoharu Seiki and Yoshifumi Itoh",
note = "Keywords: Amino Acid Motifs; Animals; CHO Cells; COS Cells; Caveolae; Cell Movement; Cercopithecus aethiops; Clathrin; Cricetinae; Cysteine; Matrix Metalloproteinase 14; Matrix Metalloproteinases; Matrix Metalloproteinases, Membrane-Associated; Mice; Palmitic Acid; Protein Processing, Post-Translational",
year = "2005",
doi = "10.1096/fj.04-3651fje",
language = "English",
volume = "19",
pages = "1326--8",
journal = "The FASEB Journal",
issn = "0892-6638",
publisher = "Federation of American Societies for Experimental Biology",
number = "10",
}