Definition of a direct extracellular interaction between Met and E‐cadherin

Reshetnikova, Galina; Troyanovsky, Sergey M.; Rimm, David L.

doi:10.1016/j.cellbi.2007.01.022

Cited by 41 publications

(34 citation statements)

References 35 publications

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“…E-cadherin also associates with c-Met, IGF1R and α vintegrin at the plasma membrane [39,40]. Interestingly, in the absence of α-catenin the E-cadherin/IGF1R complex does not form, suggesting that α-catenin besides its function as actin-anchoring protein also exerts a function as an important scaffolding protein.…”

Section: Epithelial Cell-cell Adhesionmentioning

confidence: 91%

EMT, the cytoskeleton, and cancer cell invasion

Yilmaz

Christofori

2009

Cancer Metastasis Rev

1,533

1,314

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The metastatic process, i.e. the dissemination of cancer cells throughout the body to seed secondary tumors at distant sites, requires cancer cells to leave the primary tumor and to acquire migratory and invasive capabilities. In a process of epithelial-mesenchymal transition (EMT), besides changing their adhesive repertoire, cancer cells employ developmental processes to gain migratory and invasive properties that involve a dramatic reorganization of the actin cytoskeleton and the concomitant formation of membrane protrusions required for invasive growth. The molecular processes underlying such cellular changes are still only poorly understood, and the various migratory organelles, including lamellipodia, filopodia, invadopodia and podosomes, still require a better functional and molecular characterization. Notably, direct experimental evidence linking the formation of migratory membrane protrusions and the process of EMT and tumor metastasis is still lacking. In this review, we have summarized recent novel insights into the molecular processes and players underlying EMT on one side and the formation of invasive membrane protrusions on the other side.

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Section: Epithelial Cell-cell Adhesionmentioning

confidence: 91%

EMT, the cytoskeleton, and cancer cell invasion

Yilmaz

Christofori

2009

Cancer Metastasis Rev

1,533

1,314

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“…In contrast, two tested G protein-coupled receptors were not regulated by Ecadherin. Indeed, several reports indicate that Ecadherin and receptor tyrosine kinases interact physically and colocalize at the lateral membranes of epithelial cells [190][191][192][193][194][195][196][197]. As for EGFR, formation of a complex with E-cadherin depended on the extracellular domain of E-cadherin [189,198], but was independent of p120ctn and b-catenin binding [189].…”

Section: Signaling Activities Of E-cadherinmentioning

confidence: 96%

The cell-cell adhesion molecule E-cadherin

Roy

Berx

2008

Cell. Mol. Life Sci.

1,082

808

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This review is dedicated to E-cadherin, a calcium-dependent cell-cell adhesion molecule with pivotal roles in epithelial cell behavior, tissue formation, and suppression of cancer. As founder member of the cadherin superfamily, it has been extensively investigated. We summarize the structure and regulation of the E-cadherin gene and transcript. Models for E-cadherin-catenin complexes and cell junctions are presented. The structure of the E-cadherin protein is discussed in view of the diverse functions of this remarkable protein. Homophilic and heterophilic adhesion are compared, including the role of E-cadherin as a receptor for pathogens. The complex post-translational processing of E-cadherin is reviewed, as well as the many signaling activities. The role of E-cadherin in embryonic development and morphogenesis is discussed for several animal models. Finally, we review the multiple mechanisms that disrupt E-cadherin function in cancer: inactivating somatic and germline mutations, epigenetic silencing by DNA methylation and epithelial to mesenchymal transition-inducing transcription factors, and dysregulated protein processing.

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“…Crosstalk occurs between MET and the developmental Wnt-b-catenin pathway in which MET directly interacts with E-cadherin and induces nuclear localization of b-catenin Apte et al 2006;Reshetnikova et al 2007). Recent work has shown that in colon cancer, HGF-producing myofibroblasts activate b-catenin-dependent transcription and stimulate cancer stem cell (CSC) populations (Vermeulen et al 2010).…”

Section: Gab1 Gab1 H G F / S F H G F / S F Hgf/sfmentioning

confidence: 99%

MET: A Critical Player in Tumorigenesis and Therapeutic Target

Graveel

Tolbert

Woude

2013

Cold Spring Harbor Perspectives in Biology

108

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Since its discovery more than 25 years ago, numerous studies have established that the MET receptor is unique among tyrosine kinases. Signaling through MET is necessary for normal development and for the progression of a wide range of human cancers. MET activation has been shown to drive numerous signaling pathways; however, it is not clear how MET signaling mediates diverse cellular responses such as motility, invasion, growth, and angiogenesis. Great strides have been made in understanding the pleotropic aspects of MET signaling using three-dimensional molecular structures, cell culture systems, human tumors, and animal models. These combined approaches have driven the development of MET-targeted therapeutics that have shown promising results in the clinic. Here we examine the unique features of MET and hepatocyte growth factor/scatter factor (HGF/SF) structure and signaling, mutational activation, genetic mouse models of MET and HGF/SF, and MET-targeted therapeutics.

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Definition of a direct extracellular interaction between Met and E‐cadherin

Cited by 41 publications

References 35 publications

EMT, the cytoskeleton, and cancer cell invasion

EMT, the cytoskeleton, and cancer cell invasion

The cell-cell adhesion molecule E-cadherin

MET: A Critical Player in Tumorigenesis and Therapeutic Target

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