Src-mediated Tyrosine Phosphorylation of Caveolin-1 Induces Its Association with Membrane Type 1 Matrix Metalloproteinase

Labrecque, Lyne; Nyalendo, Carine; Langlois, Stéphanie; Durocher, Yves; Roghi, Christian; Murphy, Gillian; Gingras, Denis; Béliveau, Richard

doi:10.1074/jbc.m409617200

Cited by 145 publications

(136 citation statements)

References 52 publications

(81 reference statements)

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“…13) induces activation of the G protein a i subunit with subsequent activation of Src (63). Activated Src would then stimulate MT1-MMP activity, either directly or through the tyrosine phosphorylation of caveolin-1, which allows the formation of an MT1-MMP-caveolin-1 complex (17). Through a process that involves its cytoplasmic domain, MT1-MMP would stimulate the activation of an unidentified TIMP-2 -and TIMP-3 -insensitive membrane-associated MMP or ADAM.…”

Section: Discussionmentioning

confidence: 99%

“…A plasmid encoding COOH-terminal Src kinase (Csk) was kindly provided by Dr. H. Hanafusa (Osaka Bioscience Institute, Japan), and the Csk coding sequence was subcloned at the EcoRI site of pcDNA3.1. The plasmids encoding the wild-type and constitutively active Ga i2 proteins were recently described (13,17).…”

Section: Plasmids and Transfection Methodsmentioning

confidence: 99%

“…Lysates were clarified by centrifugation at 8,000 Â g for 20 min at 4jC. The extent of EGFR phosphorylation was monitored by immunoprecipitation, essentially as described (17). Precleared supernatants (500 Ag of proteins) were incubated with EGFR or FLAG M2 antibodies overnight at 4jC with constant rocking.…”

Section: Analysis Of Egfr Transactivationmentioning

confidence: 99%

“…The overexpression of MT1-MMP enables tumor cell growth in otherwise growthrestrictive, three-dimensional extracellular matrices (7) and promotes cell migration of a number of cancer (8)(9)(10) and endothelial cell lines (11)(12)(13). The short cytoplasmic sequence of MT1-MMP also contributes to the induction of cell migration by the enzyme (9, 10, 13) possibly through activation of the extracellular signal-regulated protein kinase (ERK) cascade (14), endocytosis and trafficking of the enzyme (15,16), and interaction with tyrosine phosphorylated caveolin-1 (17). Additional insights into the mechanisms by which MT1-MMP induces cell migration may come from our observation that MT1-MMP cooperates with the plateletderived bioactive lipid sphingosine 1-phosphate (S1P) to stimulate endothelial cell migration and morphogenic differentiation into capillary-like structures in vitro (13).…”

Section: Introductionmentioning

confidence: 99%

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Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Langlois

Nyalendo

Tomasso

et al. 2007

Molecular Cancer Research

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Proteolysis of extracellular matrix proteins by membrane-type 1 matrix metalloproteinase (MT1-MMP) plays a pivotal role in tumor and endothelial cell migration. In addition to its proteolytic activity, several studies indicate that the proinvasive properties of MT1-MMP also involve its short cytoplasmic domain, but the specific mechanisms mediating this function have yet to be fully elucidated. Having previously shown that the serum factor sphingosine 1-phosphate stimulates MT1-MMP promigratory function through a process that involves its cytoplasmic domain, we now extend these findings to show that this cooperative interaction is permissive to cellular migration through MT1-MMP -dependent transactivation of the epidermal growth factor receptor (EGFR). In the presence of sphingosine 1-phosphate, MT1-MMP stimulates EGFR transactivation through a process that is dependent upon the cytoplasmic domain of the enzyme but not its catalytic activity. The MT1-MMP -induced EGFR transactivation also involves G i protein signaling and Src activities and leads to enhanced cellular migration through downstream extracellular signal-regulated kinase activation. The present study, thus, elucidates a novel role of MT1-MMP in signaling events mediating EGFR transactivation and provides the first evidence of a crucial role of this receptor activity in MT1-MMP promigratory function. Taken together, our results suggest that the inhibition of EGFR may represent a novel target to inhibit MT1-MMP -dependent processes associated with tumor cell invasion and angiogenesis. (Mol Cancer Res 2007;5(6):569 -83)

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Section: Discussionmentioning

confidence: 99%

Section: Plasmids and Transfection Methodsmentioning

confidence: 99%

Section: Analysis Of Egfr Transactivationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Langlois

Nyalendo

Tomasso

et al. 2007

Molecular Cancer Research

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“…While in vitro studies have shown that Src can regulate many different molecules including intracellular signaling intermediates, integrins, matrix metalloproteases, and ECM proteins, the specific role of Src in vivo is poorly understood [67][68][69][70][71][72][73][74][75][76]. Based on knockout studies, it is known that other Src-related family kinases can compensate for the absence of Src particularly during development.…”

Section: Discussionmentioning

confidence: 99%

Reduced Glioma Infiltration in Src-deficient Mice

et al. 2006

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SummaryMalignant brain tumors, such as glioblastoma, are characterized by extensive angiogenesis and permeability of the blood-brain barrier (BBB). The infiltration of glioma cells away from the primary tumor mass is a pathological characteristic of glial tumors. The infiltrating tumor cells represent a significant factor in tumor recurrence following surgical debulking, radiation, and chemotherapy treatments. Vascular endothelial growth factor (VEGF)-mediated vascular permeability (VP) has been associated with the progression of glioma tumor growth and infiltration into surrounding normal brain parenchyma. While VEGF induces a robust VP response in control mice (src +/+ or src +/− ), the VP response is blocked in src −/− mice that demonstrate a 'leakage-resistant phenotype' in the brain. We used the Src-deficient mouse model to determine the role of Src in the maintenance of the BBB following orthotopic implantation and growth of glioma cells in the brain. Although solid tumor growth was the same in control and src −/− mice, the infiltrating component of glioma growth was reduced in src −/− mice. Characterization of the expression and localization of the extracellular matrix (ECM) protein fibrinogen was evaluated to determine the effect of a Src-mediated VP defect in the host compartment. These studies indicate that the reduced VP of host brain blood vessels of src −/− mice mediates a reduction in glioma cell invasion in a mouse brain tumor xenograft model.

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Adhesion‐dependent Caveolin‐1 Tyrosine‐14 phosphorylation is regulated by FAK in response to changing matrix stiffness

et al. 2021

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Integrin‐mediated adhesion regulates cellular responses to changes in the mechanical and biochemical properties of the extracellular matrix. Cell–matrix adhesion regulates caveolar endocytosis, dependent on caveolin 1 (Cav1) Tyr14 phosphorylation (pY14Cav1), to control anchorage‐dependent signaling. We find that cell–matrix adhesion regulates pY14Cav1 levels in mouse fibroblasts. Biochemical fractionation reveals endogenous pY14Cav1 to be present in caveolae and focal adhesions (FA). Adhesion does not affect caveolar pY14Cav1, supporting its regulation at FA, in which PF‐228‐mediated inhibition of focal adhesion kinase (FAK) disrupts. Cell adhesion on 2D polyacrylamide matrices of increasing stiffness stimulates Cav1 phosphorylation, which is comparable to the phosphorylation of FAK. Inhibition of FAK across varying stiffnesses shows it regulates pY14Cav1 more prominently at higher stiffness. Taken together, these studies reveal the presence of FAK–pY14Cav1 crosstalk at FA, which is regulated by cell–matrix adhesion.

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Src-mediated Tyrosine Phosphorylation of Caveolin-1 Induces Its Association with Membrane Type 1 Matrix Metalloproteinase

Cited by 145 publications

References 52 publications

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Reduced Glioma Infiltration in Src-deficient Mice

Adhesion‐dependent Caveolin‐1 Tyrosine‐14 phosphorylation is regulated by FAK in response to changing matrix stiffness

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