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- W2018347222 abstract "The matrix metalloproteinase MT1-MMP has a decisive impact on invasive cell migration in both physiological and pathological settings such as immune cell extravasation or metastasis of cancer cells. Surface-associated MT1-MMP is able to cleave components of the extracellular matrix, which is a prerequisite for proteolytic invasive migration. However, current knowledge on the molecular mechanisms that regulate MT1-MMP trafficking to and from the cell surface is limited. Here, we identify three members of the RabGTPase family, Rab5a, Rab8a, and Rab14, as critical regulators of MT1-MMP trafficking and function in primary human macrophages. Both overexpressed and endogenous forms show prominent colocalisation with MT1-MMP-positive vesicles, while expression of mutant constructs as well as siRNA-induced knockdown reveal that these RabGTPases critically regulate MT1-MMP surface exposure, contact of MT1-MMP-positive vesicles with podosomes, extracellular matrix degradation in 2D and 3D, as well as 3D proteolytic invasion of macrophages. Collectively, our results identify Rab5a, Rab8a, and Rab14 as major regulators of MT1-MMP trafficking and invasive migration of primary human macrophages, pointing to them as promising potential targets for manipulation of immune cell invasion." @default.
- W2018347222 created "2016-06-24" @default.
- W2018347222 creator A5017647045 @default.
- W2018347222 creator A5034775933 @default.
- W2018347222 creator A5089862690 @default.
- W2018347222 date "2013-01-01" @default.
- W2018347222 modified "2023-10-12" @default.
- W2018347222 title "A specific subset of RabGTPases controls cell surface exposure of MT1-MMP, extracellular matrix degradation and 3D invasion of macrophages" @default.
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- W2018347222 doi "https://doi.org/10.1242/jcs.122358" @default.
- W2018347222 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23606746" @default.
- W2018347222 hasPublicationYear "2013" @default.
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