Title: Control of MT1-MMP transport by atypical PKC during breast-cancer progression
Authors: Rossé, Carine ×
Lodillinsky, Catalina
Fuhrmann, Laetitia
Nourieh, Maya
Monteiro, Pedro
Irondelle, Marie
Lagoutte, Emilie
Vacher, Sophie
Waharte, François
Paul-Gilloteaux, Perrine
Romao, Maryse
Sengmanivong, Lucie
Linch, Mark
Van Lint, Johan
Raposo, Graça
Vincent-Salomon, Anne
Bièche, Ivan
Parker, Peter J
Chavrier, Philippe #
Issue Date: May-2014
Publisher: National Academy of Sciences
Series Title: Proceedings of the National Academy of Sciences of the United States of America vol:111 issue:18 pages:E1872-9
Article number: 10.1073/pnas.1400749111
Abstract: Dissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co-up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP-containing endosomes, phosphorylates cortactin, which is present in F-actin-rich puncta on MT1-MMP-positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells.
ISSN: 0027-8424
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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