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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. / Anilkumar, Narayanapanicker; Uekita, Takamasa; Couchman, John R; Nagase, Hideaki; Seiki, Motoharu; Itoh, Yoshifumi.

In: The FASEB Journal, Vol. 19, No. 10, 2005, p. 1326-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Anilkumar, N, Uekita, T, Couchman, JR, Nagase, H, Seiki, M & Itoh, Y 2005, 'Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration.', The FASEB Journal, vol. 19, no. 10, pp. 1326-8. https://doi.org/10.1096/fj.04-3651fje

APA

Anilkumar, N., Uekita, T., Couchman, J. R., Nagase, H., Seiki, M., & Itoh, Y. (2005). Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. The FASEB Journal, 19(10), 1326-8. https://doi.org/10.1096/fj.04-3651fje

Vancouver

Anilkumar N, Uekita T, Couchman JR, Nagase H, Seiki M, Itoh Y. Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. The FASEB Journal. 2005;19(10):1326-8. https://doi.org/10.1096/fj.04-3651fje

Author

Anilkumar, Narayanapanicker ; Uekita, Takamasa ; Couchman, John R ; Nagase, Hideaki ; Seiki, Motoharu ; Itoh, Yoshifumi. / Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. In: The FASEB Journal. 2005 ; Vol. 19, No. 10. pp. 1326-8.

Bibtex

@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 = "F A S E B Journal",
issn = "0892-6638",
publisher = "Federation of American Societies for Experimental Biology",
number = "10",

}

RIS

TY - JOUR

T1 - Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration.

AU - Anilkumar, Narayanapanicker

AU - Uekita, Takamasa

AU - Couchman, John R

AU - Nagase, Hideaki

AU - Seiki, Motoharu

AU - Itoh, Yoshifumi

N1 - 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

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

U2 - 10.1096/fj.04-3651fje

DO - 10.1096/fj.04-3651fje

M3 - Journal article

C2 - 15946988

VL - 19

SP - 1326

EP - 1328

JO - F A S E B Journal

JF - F A S E B Journal

SN - 0892-6638

IS - 10

ER -

ID: 5160926