v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at β1 Integrin-containing Invadopodia Promotes Cell Invasion*
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Summary
It is established that gain-of-function v-Src SH3 targeting interactions with FAK at β1 integrin-containing invadopodia act to stabilize a v- Src·FAK signaling complex promoting cell invasion.
- Type
- article
- Published
- 2002-04-12
- Cited by
- 125
- References
- 28
- Access
- Open access
- OpenAlex
- https://openalex.org/W1964075433
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:11459134
Keywords
Invadopodia, Focal adhesion, Proto-oncogene tyrosine-protein kinase Src, Integrin, Cell biology
References
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- Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein
- Cellular invasion into matrix beads: localization of beta 1 integrins and fibronectin to the invadopodia.
- Tyrosine Phosphorylation of Connexin 43 by v-Src Is Mediated by SH2 and SH3 Domain Interactions*
- The v-Src SH3 Domain Facilitates a Cell Adhesion-independent Association with Focal Adhesion Kinase*
- c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism.
- Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions.
- Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro.
- DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
- Signaling through focal adhesion kinase.
- Biochemical signals and biological responses elicited by the focal adhesion kinase.
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- pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.
- Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
- Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
- Activation of β1 Integrin Signaling Stimulates Tyrosine Phosphorylation of p190 RhoGAP and Membrane-protrusive Activities at Invadopodia*
- Pyk2 and Src‐family protein‐tyrosine kinases compensate for the loss of FAK in fibronectin‐stimulated signaling events but Pyk2 does not fully function to enhance FAK− cell migration
- Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins
Cited by
- FAK expression regulation and therapeutic potential.
- Implication des voies de signalisation de l'adhérence cellulaire dans le contrôle de l'hypoxie tumorale des glioblastomes
- Cell and molecular biology of invadopodia.
- Role of ARF6 in breast cancer cell invasion
- Control of cAMP signalling in the cellular migration of pancreatic ductal adenocarcinoma
- IGF-1 receptor transactivation mediates Src-dependent cortactin phosphorylation in response to angiotensin II.
- Étude de l'implication du système protéolytique neutre calcium-dépendant dans la migration des cellules musculaires tumorales
- Evaluation of focal adhesion kinase as a novel radiosensitising target
- Reactive oxygen species in tumor progression.
- The role of the exocyst in exocytosis and cell migration
- Repression of Protein Kinase C delta in human squamous cell carcinomas by Ras, Fyn and NF-kappa B signaling
- Integrin adhesion receptors in tumor metastasis
- Podosomes and Invadopodia: Related structures with Common Protein Components that May Promote Breast Cancer Cellular Invasion
- The role of Twist1 in promoting tumor invasion and metastasis by regulation of invadopodia formation
- SH3 domain of c‐Src governs its dynamics at focal adhesions and the cell membrane
- The role of Src kinase in renal cell carcinoma
- Understanding the Roles of FAK in Cancer
- Aiming for invadopodia: organizing polarized delivery at sites of invasion.
- Src and FAK mediate cell–matrix adhesion‐dependent activation of met during transformation of breast epithelial cells
- Focal adhesion kinase overexpression: Correlation with lymph node metastasis and shorter survival in oral squamous cell carcinoma
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- Inhibiting FAK–Paxillin Interaction Reduces Migration and Invadopodia-Mediated Matrix Degradation in Metastatic Melanoma Cells
- Focal Adhesion Kinases in Adhesion Structures and Disease
- Laminin-332-β1 Integrin Interactions Negatively Regulate Invadopodia
- Requirements for localization of p130cas to focal adhesions