Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia

Poincloux, Renaud; Lizárraga, Floria; Chavrier, Philippe

doi:10.1242/jcs.034561

Cited by 431 publications

(438 citation statements)

References 135 publications

(216 reference statements)

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“…Surface MT1-MMP is internalized by clathrin-and caveolin-dependent endocytosis and is then degraded in lysosomes or recycled back to the plasma membrane (27). Recent studies have revealed that the targeted delivery of MT1-MMP to invadopodia through membrane trafficking is necessary for its accumulation and proteolytic activity in these structures (21,22,30,31). In addition, we previously reported that caveolin-1 colocalizes and traffics with MT1-MMP and controls the MT1-MMP-dependent degradation of the ECM at invadopodia (29).…”

Section: Discussionmentioning

confidence: 99%

“…Recent studies have shown that targeted trafficking of MT1-MMP to invadopodia, which is mediated by vesicleassociated membrane protein 7, the exocyst complex, caveolin-1, and lipid rafts, is crucial for its accumulation and matrix degradation activity at invadopodia (21,22,(29)(30)(31). Therefore, we next examined the effect of CDCP1 knockdown on the localization of MT1-MMP at invadopodia.…”

Section: Cdcp1 Regulates Mt1-mmp-dependent Invasionmentioning

confidence: 99%

“…The matrix degradation activity at invadopodia is dependent on the accumulation and activation of MT1-MMP at the cell surface of invadopodia (26)(27)(28). Recent studies have revealed that endocytic and exocytic trafficking are critical for the targeted delivery of MT1-MMP to invadopodia (21,(29)(30)(31). However, the molecular mechanisms that control the delivery and function of MT1-MMP at invadopodia are not fully understood.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

Miyazawa

Uekita

Ito

et al. 2013

Molecular Cancer Research

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Complement C1r/C1s, Uegf, Bmp1 (CUB) domain-containing protein 1 (CDCP1) is a transmembrane protein that regulates anchorage-independent growth and cancer cell migration and invasion. Expression of CDCP1 is detected in a number of cancer cell lines and tissues and is closely correlated with poor prognosis. Invadopodia are actin-based protrusions on the surface of invasive cancer cells that promote the degradation of the extracellular matrix (ECM) via localized proteolysis, which is mainly mediated by membrane type 1 matrix metalloproteinase (MT1-MMP). MT1-MMP is accumulated at invadopodia by targeted delivery via membrane trafficking. The present study shows that CDCP1 is required for ECM degradation by invadopodia in human breast cancer and melanoma cells. CDCP1 localized to caveolin-1-containing vesicular structures and lipid rafts and was detected in close proximity to invadopodia. Further biochemical analysis revealed that substantial amounts of CDCP1 existed in the Triton X-100 insoluble lipid raft fraction. CDCP1 was coimmunoprecipitated with MT1-MMP and colocalized with MT1-MMP at the vesicular structures. The siRNA-mediated knockdown of the CDCP1 expression markedly inhibited MT1-MMP-dependent ECM degradation and Matrigel invasion and reduced the accumulation of MT1-MMP at invadopodia, as shown by immunofluorescence analysis. These results indicate that CDCP1 is an essential regulator of the trafficking and function of MT1-MMP-and invadopodia-mediated invasion of cancer cells. Mol Cancer Res; 11(6); 628-37.

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Section: Discussionmentioning

confidence: 99%

Section: Cdcp1 Regulates Mt1-mmp-dependent Invasionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

Miyazawa

Uekita

Ito

et al. 2013

Molecular Cancer Research

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“…Delivery of MT1-MMP to the invadosome further requires the master regulators of endocytosis Rab5 and Rab4 [118], as well as a vSNARE and VAMP7 for fusing the MT1-MMP-containing vesicles with the plasma membrane and presumably Rab8 for exocytosis [119]. Notably, overexpression of Rab5 in cancer cells was found to be necessary and sufficient for cell invasion and tumor dissemination by enhancing MT1-MMP driven extracellular matrix degradation and increasing intratumoral cell motility [118].…”

Section: Trafficking Of Other Cell Surface Adhesions Proteinsmentioning

confidence: 99%

On the move: endocytic trafficking in cell migration

Maritzen

Schachtner

Legler

2015

Cell. Mol. Life Sci.

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Directed cell migration is a fundamental process underlying diverse physiological and pathophysiological phenomena ranging from wound healing and induction of immune responses to cancer metastasis. Recent advances reveal that endocytic trafficking contributes to cell migration in multiple ways. (1) At the level of chemokines and chemokine receptors: internalization of chemokines by scavenger receptors is essential for shaping chemotactic gradients in tissue, whereas endocytosis of chemokine receptors and their subsequent recycling is key for maintaining a high responsiveness of migrating cells. (2) At the level of integrin trafficking and focal adhesion dynamics: endosomal pathways do not only modulate adhesion by delivering integrins to their site of action, but also by supplying factors for focal adhesion disassembly. (3) At the level of extracellular matrix reorganization: endosomal transport contributes to tumor cell migration not only by targeting integrins to invadosomes but also by delivering membrane type 1 matrix metalloprotease to the leading edge facilitating proteolysis-dependent chemotaxis. Consequently, numerous endocytic and endosomal factors have been shown to modulate cell migration. In fact key modulators of endocytic trafficking turn out to be also key regulators of cell migration. This review will highlight the recent progress in unraveling the contribution of cellular trafficking pathways to cell migration.

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“…Invadopodia are cell-matrix contacts, similar to focal adhesions, established in the context of "invading" cellular protusions [66]. Invadopodia can promote ECM proteolysis through their associated proteases, particularly MT1-MMP [67], and thus have been implicated in cancer invasion, both neoplastic cells moving out and cancer-associated fibroblasts moving in [66]. The cause and consequences of invadopodia unites many of the key themes from the discussion above, including ECM remodeling, matrix proteases, cell motility and mechanical forces [66].…”

Section: Remodeling Of the Bm And Ecm In Cancermentioning

confidence: 99%

The Extracellular Matrix in Digestive Cancer

Worthley

Giraud

Wang

2010

Cancer Microenvironment

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The extracellular components of the cancer microenvironment play a critical role in tumor initiation, progression and invasion. In this review we examine the normal formation and function of the basement membrane and extracellular matrix. We characterize the interactions between the matrix and the epithelium and explore the causes and consequences of the extracellular remodeling that accompanies carcinogenesis. Finally, we address the therapeutic possibilities of incorporating matrix as well as epithelial strategies in the management of digestive cancer.

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Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia

Cited by 431 publications

References 135 publications

CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

CDCP1 Regulates the Function of MT1-MMP and Invadopodia-Mediated Invasion of Cancer Cells

On the move: endocytic trafficking in cell migration

The Extracellular Matrix in Digestive Cancer

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