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1.
bioRxiv ; 2024 May 13.
Article in English | MEDLINE | ID: mdl-38798670

ABSTRACT

Endothelia cells respond to mechanical force by stimulating cellular signaling, but how these pathways are linked to elevations in cell metabolism and whether metabolism supports the mechanical response remains poorly understood. Here, we show that application of force to VE-cadherin stimulates liver kinase B1 (LKB1) to activate AMP-activated protein kinase (AMPK), a master regulator of energy homeostasis. VE-cadherin stimulated AMPK increases eNOS activity and localization to the plasma membrane as well as reinforcement of the actin cytoskeleton and cadherin adhesion complex, and glucose uptake. We present evidence for the increase in metabolism being necessary to fortify the adhesion complex, actin cytoskeleton, and cellular alignment. Together these data extend the paradigm for how mechanotransduction and metabolism are linked to include a connection to vasodilation, thereby providing new insight into how diseases involving contractile, metabolic, and vasodilatory disturbances arise.

2.
Curr Opin Cell Biol ; 84: 102219, 2023 10.
Article in English | MEDLINE | ID: mdl-37651955

ABSTRACT

Epithelial and endothelial cells experience numerous mechanical cues throughout their lifetimes. Cells resist these forces by fortifying their cytoskeletal networks and adhesions. This reinforcement is energetically costly. Here we describe how these energetic demands are met. We focus on the response of epithelial and endothelial cells to mechanical cues, describe the energetic needs of epithelia and endothelia, and identify the mechanisms these cells employ to increase glycolysis, oxidative phosphorylation, and fatty acid metabolism. We discuss the similarities and differences in the responses of the two cell types.


Subject(s)
Endothelial Cells , Mechanotransduction, Cellular , Lipid Metabolism , Cues , Cytoskeleton
3.
J Cell Sci ; 136(12)2023 06 15.
Article in English | MEDLINE | ID: mdl-37248996

ABSTRACT

Vinculin is an actin-binding protein present at cell-matrix and cell-cell adhesions, which plays a critical role in bearing force experienced by cells and dissipating it onto the cytoskeleton. Recently, we identified a key tyrosine residue, Y822, whose phosphorylation plays a critical role in force transmission at cell-cell adhesions. The role of Y822 in human cancer remains unknown, even though Y822 is mutated to Y822C in uterine cancers. Here, we investigated the effect of this amino acid substitution and that of a phosphodeficient Y822F vinculin in cancer cells. We observed that the presence of the Y822C mutation led to cells that proliferate and migrate more rapidly and contained smaller focal adhesions when compared to cells with wild-type vinculin. In contrast, the presence of the Y822F mutation led to highly spread cells with larger focal adhesions and increased contractility. Furthermore, we provide evidence that Y822C vinculin forms a disulfide bond with paxillin, accounting for some of the elevated phosphorylated paxillin recruitment. Taken together, these data suggest that vinculin Y822 modulates the recruitment of ligands.


Subject(s)
Cell Communication , Focal Adhesions , Humans , Vinculin/genetics , Vinculin/metabolism , Paxillin/genetics , Paxillin/metabolism , Ligands , Cell Adhesion/genetics , Focal Adhesions/genetics , Focal Adhesions/metabolism
4.
Biol Cell ; 115(5): e202200108, 2023 May.
Article in English | MEDLINE | ID: mdl-36807920

ABSTRACT

Much attention has been dedicated to understanding how cells sense and respond to mechanical forces. The types of forces cells experience as well as the repertoire of cell surface receptors that sense these forces have been identified. Key mechanisms for transmitting that force to the cell interior have also emerged. Yet, how cells process mechanical information and integrate it with other cellular events remains largely unexplored. Here we review the mechanisms underlying mechanotransduction at cell-cell and cell-matrix adhesions, and we summarize the current understanding of how cells integrate information from the distinct adhesion complexes with cell metabolism.


Subject(s)
Cell-Matrix Junctions , Mechanotransduction, Cellular , Cell Adhesion , Mechanotransduction, Cellular/physiology , Cell-Matrix Junctions/metabolism
5.
J Invest Dermatol ; 142(2): 314-322, 2022 02.
Article in English | MEDLINE | ID: mdl-34310950

ABSTRACT

IRF6 is a transcription factor that is required for craniofacial development and epidermal morphogenesis. Specifically, Irf6-deficient mice lack the terminally differentiated epidermal layers, leading to an absence of barrier function. This phenotype also includes intraoral adhesions due to the absence of the oral periderm, leading to the mislocalization of E-cadherin and other cell‒cell adhesion proteins of the oral epithelium. However, the mechanisms by which IRF6 controls the localization of cell adhesion proteins are not understood. In this study, we show that in human and murine keratinocytes, loss of IRF6 leads to a breakdown of epidermal sheets after mechanical stress. This defect is due to a reduction of adhesion proteins at the plasma membrane. Dynamin inhibitors rescued the IRF6-dependent resistance of epidermal sheets to mechanical stress, but only inhibition of clathrin-mediated endocytosis rescued the localization of junctional proteins at the membrane. Our data show that E-cadherin recycling but not its endocytosis is affected by loss of IRF6. Overall, we demonstrate a role for IRF6 in the delivery of adhesion proteins to the cell membrane.


Subject(s)
Antigens, CD/metabolism , Cadherins/metabolism , Interferon Regulatory Factors/metabolism , Animals , Cell Adhesion/drug effects , Cell Line , Cell Membrane/drug effects , Cell Membrane/metabolism , Dynamins/antagonists & inhibitors , Dynamins/metabolism , Endocytosis/drug effects , Gene Knockdown Techniques , Humans , Hydrazones/pharmacology , Intercellular Junctions/drug effects , Intercellular Junctions/metabolism , Interferon Regulatory Factors/genetics , Keratinocytes/drug effects , Keratinocytes/metabolism , Mice , Naphthols/pharmacology , Primary Cell Culture , Stress, Mechanical
6.
Nat Cell Biol ; 23(5): 457-466, 2021 05.
Article in English | MEDLINE | ID: mdl-33972734

ABSTRACT

The response of cells to forces is critical for their function and occurs via rearrangement of the actin cytoskeleton1. Cytoskeletal remodelling is energetically costly2,3, yet how cells signal for nutrient uptake remains undefined. Here we present evidence that force transmission increases glucose uptake by stimulating glucose transporter 1 (GLUT1). GLUT1 recruitment to and retention at sites of force transmission requires non-muscle myosin IIA-mediated contractility and ankyrin G. Ankyrin G forms a bridge between the force-transducing receptors and GLUT1. This bridge is critical for enabling cells under tension to tune glucose uptake to support remodelling of the actin cytoskeleton and formation of an epithelial barrier. Collectively, these data reveal an unexpected mechanism for how cells under tension take up nutrients and provide insight into how defects in glucose transport and mechanics might be linked.


Subject(s)
Ankyrins/metabolism , Biological Transport/physiology , Cell Membrane/metabolism , Glucose/metabolism , Carrier Proteins/metabolism , Cytoskeleton/metabolism , Glucose Transporter Type 1/metabolism , Humans , Signal Transduction/physiology
7.
J Cell Sci ; 134(3)2021 02 08.
Article in English | MEDLINE | ID: mdl-33558441

ABSTRACT

Attention has long focused on the actin cytoskeleton as a unit capable of organizing into ensembles that control cell shape, polarity, migration and the establishment of intercellular contacts that support tissue architecture. However, these investigations do not consider observations made over 40 years ago that the actin cytoskeleton directly binds metabolic enzymes, or emerging evidence suggesting that the rearrangement and assembly of the actin cytoskeleton is a major energetic drain. This Review examines recent studies probing how cells adjust their metabolism to provide the energy necessary for cytoskeletal remodeling that occurs during cell migration, epithelial to mesenchymal transitions, and the cellular response to external forces. These studies have revealed that mechanotransduction, cell migration, and epithelial to mesenchymal transitions are accompanied by alterations in glycolysis and oxidative phosphorylation. These metabolic changes provide energy to support the actin cytoskeletal rearrangements necessary to allow cells to assemble the branched actin networks required for cell movement and epithelial to mesenchymal transitions and the large actin bundles necessary for cells to withstand forces. In this Review, we discuss the emerging evidence suggesting that the regulation of these events is highly complex with metabolism affecting the actin cytoskeleton and vice versa.


Subject(s)
Actins , Mechanotransduction, Cellular , Actin Cytoskeleton/metabolism , Actins/metabolism , Cell Movement , Cytoskeleton/metabolism
8.
Biology (Basel) ; 11(1)2021 Dec 30.
Article in English | MEDLINE | ID: mdl-35053050

ABSTRACT

The shape of cells is altered to allow cells to adapt to their changing environments, including responding to internally generated and externally applied force. Force is sensed by cell surface adhesion proteins that are enriched in sites where cells bind to the extracellular matrix (focal adhesions) and neighboring cells (cell-cell or adherens junctions). Receptors at these adhesion sites stimulate intracellular signal transduction cascades that culminate in dramatic changes in the actin cytoskeleton. New actin filaments form, and/or new and existing filaments can be cleaved, branched, or bundled. Here, we discuss the actin cytoskeleton and its functions. We will examine the current understanding for how the actin cytoskeleton is tethered to adhesion sites. Finally, we will highlight recent studies describing how the actin cytoskeleton at these adhesion sites is remodeled in response to force.

9.
J Virol ; 94(9)2020 04 16.
Article in English | MEDLINE | ID: mdl-32102878

ABSTRACT

Semen is the primary transmission vehicle for various pathogenic viruses. Initial steps of transmission, including cell attachment and entry, likely occur in the presence of semen. However, the unstable nature of human seminal plasma and its toxic effects on cells in culture limit the ability to study in vitro virus infection and inhibition in this medium. We found that whole semen significantly reduces the potency of antibodies and microbicides that target glycans on the envelope glycoproteins (Envs) of HIV-1. The extraordinarily high concentration of the monosaccharide fructose in semen contributes significantly to the effect by competitively inhibiting the binding of ligands to α1,2-linked mannose residues on Env. Infection and inhibition in whole human seminal plasma are accurately mimicked by a stable synthetic simulant of seminal fluid that we formulated. Our findings indicate that, in addition to the protein content of biological secretions, their small-solute composition impacts the potency of antiviral microbicides and mucosal antibodies.IMPORTANCE Biological secretions allow viruses to spread between individuals. Each type of secretion has a unique composition of proteins, salts, and sugars, which can affect the infectivity potential of the virus and inhibition of this process. Here, we describe HIV-1 infection and inhibition in whole human seminal plasma and a synthetic simulant that we formulated. We discovered that the sugar fructose in semen decreases the activity of a broad and potent class of antiviral agents that target mannose sugars on the envelope protein of HIV-1. This effect of semen fructose likely reduces the efficacy of such inhibitors to prevent the sexual transmission of HIV-1. Our findings suggest that the preclinical evaluation of microbicides and vaccine-elicited antibodies will be improved by their in vitro assessment in synthetic formulations that simulate the effects of semen on HIV-1 infection and inhibition.


Subject(s)
Fructose/metabolism , Fructose/pharmacology , Semen/metabolism , Adult , Anti-Infective Agents/pharmacology , Antiviral Agents/antagonists & inhibitors , Antiviral Agents/pharmacology , Cell Line, Tumor , Gene Products, env/metabolism , Genes, env/genetics , HEK293 Cells , HIV Infections/virology , HIV-1/immunology , Humans , Male , Mannose/metabolism , Polysaccharides/immunology , Polysaccharides/metabolism , Semen/virology , env Gene Products, Human Immunodeficiency Virus/metabolism
10.
J Cell Biol ; 218(6): 1958-1971, 2019 06 03.
Article in English | MEDLINE | ID: mdl-30940647

ABSTRACT

Too little or too much force can trigger cell death, yet factors that ensure the survival of cells remain largely unknown. Here, we demonstrate that E-cadherin responds to force by recruiting and activating p21-activated protein kinase 2 (PAK2) to allow cells to stiffen, metabolize, and survive. Interestingly, PAK2 activation and its control of the apoptotic response are specific for the amplitude of force applied. Specifically, under low amplitudes of physiological force, PAK2 is protected from proteolysis, thereby ensuring cell survival. In contrast, under higher amplitudes of physiological force, PAK2 is left unprotected and stimulates apoptosis, an effect that is prevented by cleavage-resistant forms of the protein. Finally, we demonstrate that PAK2 protection is conferred by direct binding of AMPK. Thus, PAK2 mediates the survival of cells under force. These findings reveal an unexpected paradigm for how mechanotransduction, metabolism, and cell survival are linked.


Subject(s)
Apoptosis , Breast/cytology , Breast/metabolism , Mechanotransduction, Cellular , p21-Activated Kinases/metabolism , AMP-Activated Protein Kinases/genetics , AMP-Activated Protein Kinases/metabolism , Antigens, CD/genetics , Antigens, CD/metabolism , Cadherins/genetics , Cadherins/metabolism , Cell Adhesion , Cell Survival , Cells, Cultured , Female , Humans , Phosphorylation , Proto-Oncogene Proteins c-abl/genetics , Proto-Oncogene Proteins c-abl/metabolism , p21-Activated Kinases/genetics
11.
J Cell Sci ; 131(24)2018 12 14.
Article in English | MEDLINE | ID: mdl-30478196

ABSTRACT

The response of cells to mechanical inputs is a key determinant of cell behavior. In response to external forces, E-cadherin initiates signal transduction cascades that allow the cell to modulate its contractility to withstand the force. Much attention has focused on identifying the E-cadherin signaling pathways that promote contractility, but the negative regulators remain undefined. In this study, we identify SHP-2 as a force-activated phosphatase that negatively regulates E-cadherin force transmission by dephosphorylating vinculin Y822. To specifically probe a role for SHP-2 in E-cadherin mechanotransduction, we mutated vinculin so that it retains its phosphorylation but cannot be dephosphorylated. Cells expressing the mutant vinculin have increased contractility. This work provides a mechanism for inactivating E-cadherin mechanotransduction and provides a new method for specifically targeting the action of phosphatases in cells.


Subject(s)
Cadherins/metabolism , Protein Tyrosine Phosphatase, Non-Receptor Type 11/metabolism , Vinculin/metabolism , alpha Catenin/metabolism , Actins/metabolism , Cell Adhesion/physiology , Cytoskeleton/metabolism , Humans , Mechanotransduction, Cellular/physiology , Phosphorylation
12.
Curr Opin Cell Biol ; 54: 114-120, 2018 10.
Article in English | MEDLINE | ID: mdl-29902730

ABSTRACT

Throughout their lifetimes, all cells experience force. These forces are sensed by cell surface adhesion receptors, such as the cadherins and integrins. Much attention has focused on identifying how these adhesion receptors transmit force. In contrast, less is known regarding how these force-activated pathways are integrated with other cellular processes. In this review, we describe how cadherins and integrins transmit force, and discuss how these adhesion receptors are linked to cell metabolism. We focus on understanding this connection by highlighting how the cadherins and integrins interact with a master regulator of energy homeostasis, AMP-activated protein kinase (AMPK) and its upstream activator, Liver Kinase B1 (LKB1). We consider why there is a need for force transmission to be coupled to metabolism and highlight the major unanswered questions in the field.


Subject(s)
Cells/metabolism , Mechanotransduction, Cellular , AMP-Activated Protein Kinases/metabolism , Animals , Cell Adhesion Molecules/metabolism , Cell-Matrix Junctions/metabolism , Humans , Signal Transduction
14.
Nat Cell Biol ; 19(6): 724-731, 2017 Jun.
Article in English | MEDLINE | ID: mdl-28553939

ABSTRACT

The response of cells to mechanical force is a major determinant of cell behaviour and is an energetically costly event. How cells derive energy to resist mechanical force is unknown. Here, we show that application of force to E-cadherin stimulates liver kinase B1 (LKB1) to activate AMP-activated protein kinase (AMPK), a master regulator of energy homeostasis. LKB1 recruits AMPK to the E-cadherin mechanotransduction complex, thereby stimulating actomyosin contractility, glucose uptake and ATP production. The increase in ATP provides energy to reinforce the adhesion complex and actin cytoskeleton so that the cell can resist physiological forces. Together, these findings reveal a paradigm for how mechanotransduction and metabolism are linked and provide a framework for understanding how diseases involving contractile and metabolic disturbances arise.


Subject(s)
AMP-Activated Protein Kinases/metabolism , Cadherins/metabolism , Energy Metabolism , Mechanotransduction, Cellular , AMP-Activated Protein Kinase Kinases , AMP-Activated Protein Kinases/genetics , Actin Cytoskeleton/metabolism , Actomyosin/metabolism , Adenosine Triphosphate/metabolism , Animals , Antigens, CD , Dogs , Enzyme Activation , Glucose/metabolism , Homeostasis , Humans , Madin Darby Canine Kidney Cells , Protein Serine-Threonine Kinases/genetics , Protein Serine-Threonine Kinases/metabolism , RNA Interference , Stress, Mechanical , Transfection
15.
Exp Cell Res ; 358(1): 39-44, 2017 09 01.
Article in English | MEDLINE | ID: mdl-28372972

ABSTRACT

Cell-cell adhesions are critical for the development and maintenance of tissues. Present at sites of cell-cell contact are the adherens junctions and tight junctions. The adherens junctions mediate cell-cell adhesion via the actions of nectins and cadherins. The tight junctions regulate passage of ions and small molecules between cells and establish cell polarity. Historically, the adherens and tight junctions have been thought of as discrete complexes. However, it is now clear that a high level of interdependency exists between the two junctional complexes. The adherens junctions and tight junctions are physically linked, by the zonula occludens proteins, and linked via signaling molecules including several polarity complexes and actin cytoskeletal modifiers. This review will first describe the individual components of both the adherens and tight junctions and then discuss the coupling of the two complexes with an emphasis on the signaling links and physical interactions between the two junctional complexes.


Subject(s)
Adherens Junctions/metabolism , Cadherins/metabolism , Cell Membrane/metabolism , Cytoskeleton/metabolism , Tight Junctions/metabolism , Animals , Cell Polarity/physiology , Humans
16.
Cell Mol Life Sci ; 74(16): 2999-3009, 2017 08.
Article in English | MEDLINE | ID: mdl-28401269

ABSTRACT

Vinculin was identified as a component of focal adhesions and adherens junctions nearly 40 years ago. Since that time, remarkable progress has been made in understanding its activation, regulation and function. Here we discuss the current understanding of the roles of vinculin in cell-cell and cell-matrix adhesions. Emphasis is placed on the how vinculin is recruited, activated and regulated. We also highlight the recent understanding of how vinculin responds to and transmits force at integrin- and cadherin-containing adhesion complexes to the cytoskeleton. Furthermore, we discuss roles of vinculin in binding to and rearranging the actin cytoskeleton.


Subject(s)
Actin Cytoskeleton/metabolism , Adherens Junctions/metabolism , Cadherins/metabolism , Focal Adhesions/metabolism , Integrins/metabolism , Vinculin/metabolism , Animals , Cell Adhesion , Cell Movement , Humans , Mechanotransduction, Cellular , Models, Molecular , Protein Interaction Maps , Vinculin/analysis
17.
Biochem J ; 465(3): 383-93, 2015 Feb 01.
Article in English | MEDLINE | ID: mdl-25358683

ABSTRACT

Vinculin binding to actin filaments is thought to be critical for force transduction within a cell, but direct experimental evidence to support this conclusion has been limited. In the present study, we found mutation (R1049E) of the vinculin tail impairs its ability to bind F-actin, stimulate actin polymerization, and bundle F-actin in vitro. Further, mutant (R1049E) vinculin expressing cells are altered in cell migration, which is accompanied by changes in cell adhesion, cell spreading and cell generation of traction forces, providing direct evidence for the critical role of vinculin in mechanotransduction at adhesion sites. Lastly, we discuss the viability of models detailing the F-actin-binding surface on vinculin in the context of our mutational analysis.


Subject(s)
Actins/metabolism , Cell Movement/physiology , Mechanotransduction, Cellular/physiology , Vinculin/metabolism , Actin Cytoskeleton/chemistry , Actin Cytoskeleton/metabolism , Actins/chemistry , Animals , Mice , Mice, Knockout , Protein Binding/physiology , Protein Structure, Secondary , Vinculin/chemistry
18.
Biochemistry ; 53(49): 7706-17, 2014 Dec 16.
Article in English | MEDLINE | ID: mdl-25474123

ABSTRACT

All cells are subjected to mechanical forces throughout their lifetimes. These forces are sensed by cell surface adhesion receptors and trigger robust actin cytoskeletal rearrangements and growth of the associated adhesion complex to counter the applied force. In this review, we discuss how integrins and cadherins sense force and transmit these forces into the cell interior. We focus on the complement of proteins each adhesion complex recruits to bear the force and the signal transduction pathways activated to allow the cell to tune its contractility. A discussion of the similarities, differences, and crosstalk between cadherin- and integrin-mediated force transmission is also presented.


Subject(s)
Cell-Matrix Junctions/physiology , Extracellular Matrix/physiology , Intercellular Junctions/physiology , Mechanotransduction, Cellular , Models, Biological , Animals , Cadherins/chemistry , Cadherins/metabolism , Cell Adhesion , Cell Communication , Humans , Integrins/chemistry , Integrins/metabolism
19.
Breast Cancer Res ; 16(6): 493, 2014 Dec 13.
Article in English | MEDLINE | ID: mdl-25499888

ABSTRACT

INTRODUCTION: Several innate immunity genes are overexpressed in human cancers and their roles remain controversial. Bone marrow stromal antigen 2 (BST-2) is one such gene whose role in cancer is not clear. BST-2 is a unique innate immunity gene with both antiviral and pro-tumor functions and therefore can serve as a paradigm for understanding the roles of other innate immunity genes in cancers. METHODS: Meta-analysis of tumors from breast cancer patients obtained from the Gene Expression Omnibus (GEO) and The Cancer Genome Atlas (TCGA) datasets were evaluated for levels of BST-2 expression and for tumor aggressiveness. In vivo, we examined the effect of knockdown of BST-2 in two different murine carcinoma cells on tumor growth, metastasis, and survival. In vitro, we assessed the effect of carcinoma cell BST-2 knockdown and/or overexpression on adhesion, anchorage-independent growth, migration, and invasion. RESULTS: BST-2 in breast tumors and mammary cancer cells is a strong predictor of tumor size, tumor aggressiveness, and host survival. In humans, BST-2 mRNA is elevated in metastatic and invasive breast tumors. In mice, orthotopic implantation of mammary tumor cells lacking BST-2 increased tumor latency, decreased primary tumor growth, reduced metastases to distal organs, and prolonged host survival. Furthermore, we found that the cellular basis for the role of BST-2 in promoting tumorigenesis include BST-2-directed enhancement in cancer cell adhesion, anchorage-independency, migration, and invasion. CONCLUSIONS: BST-2 contributes to the emergence of neoplasia and malignant progression of breast cancer. Thus, BST-2 may (1) serve as a biomarker for aggressive breast cancers, and (2) be a novel target for breast cancer therapeutics.


Subject(s)
Antigens, CD/genetics , Breast Neoplasms/genetics , Carcinoma/genetics , Membrane Glycoproteins/genetics , RNA, Messenger/metabolism , Animals , Antigens, CD/metabolism , Breast Neoplasms/metabolism , Breast Neoplasms/pathology , Carcinoma/metabolism , Carcinoma/pathology , Cell Line, Tumor , Databases, Factual , Female , GPI-Linked Proteins/genetics , GPI-Linked Proteins/metabolism , Humans , Membrane Glycoproteins/metabolism , Mice , Neoplasm Invasiveness , Neoplasm Metastasis , Neoplasm Transplantation , Prognosis
20.
J Cell Biol ; 205(2): 251-63, 2014 Apr 28.
Article in English | MEDLINE | ID: mdl-24751539

ABSTRACT

Cells experience mechanical forces throughout their lifetimes. Vinculin is critical for transmitting these forces, yet how it achieves its distinct functions at cell-cell and cell-matrix adhesions remains unanswered. Here, we show vinculin is phosphorylated at Y822 in cell-cell, but not cell-matrix, adhesions. Phosphorylation at Y822 was elevated when forces were applied to E-cadherin and was required for vinculin to integrate into the cadherin complex. The mutation Y822F ablated these activities and prevented cells from stiffening in response to forces on E-cadherin. In contrast, Y822 phosphorylation was not required for vinculin functions in cell-matrix adhesions, including integrin-induced cell stiffening. Finally, forces applied to E-cadherin activated Abelson (Abl) tyrosine kinase to phosphorylate vinculin; Abl inhibition mimicked the loss of vinculin phosphorylation. These data reveal an unexpected regulatory mechanism in which vinculin Y822 phosphorylation determines whether cadherins transmit force and provides a paradigm for how a shared component of adhesions can produce biologically distinct functions.


Subject(s)
Cell Communication/physiology , Extracellular Matrix/metabolism , Mechanotransduction, Cellular/physiology , Vinculin/metabolism , Cadherins/genetics , Cadherins/metabolism , Cell Adhesion/physiology , Cell Line, Tumor , Extracellular Matrix/genetics , Humans , Phosphorylation/physiology , Proto-Oncogene Proteins c-abl/genetics , Proto-Oncogene Proteins c-abl/metabolism , Vinculin/genetics
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