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Relevant bibliographies by topics / Focal Adhesion Protein-Tyrosine Kinases

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Academic literature on the topic 'Focal Adhesion Protein-Tyrosine Kinases'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Focal Adhesion Protein-Tyrosine Kinases"

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Brown, Michael C., Leslie A. Cary, Jennifer S. Jamieson, Jonathan A. Cooper, and Christopher E. Turner. "Src and FAK Kinases Cooperate to Phosphorylate Paxillin Kinase Linker, Stimulate Its Focal Adhesion Localization, and Regulate Cell Spreading and Protrusiveness." Molecular Biology of the Cell 16, no. 9 (2005): 4316–28. http://dx.doi.org/10.1091/mbc.e05-02-0131.

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The ArfGAP paxillin kinase linker (PKL)/G protein-coupled receptor kinase-interacting protein (GIT)2 has been implicated in regulating cell spreading and motility through its transient recruitment of the p21-activated kinase (PAK) to focal adhesions. The Nck-PAK-PIX-PKL protein complex is recruited to focal adhesions by paxillin upon integrin engagement and Rac activation. In this report, we identify tyrosine-phosphorylated PKL as a protein that associates with the SH3-SH2 adaptor Nck, in a Src-dependent manner, after cell adhesion to fibronectin. Both cell adhesion and Rac activation stimulat

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Tobe, K., H. Sabe, T. Yamamoto, et al. "Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins." Molecular and Cellular Biology 16, no. 9 (1996): 4765–72. http://dx.doi.org/10.1128/mcb.16.9.4765.

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Insulin has pleiotropic effects on the regulation of cell physiology through binding to its receptor. The wide variety of tyrosine phosphorylation motifs of insulin receptor substrate 1 (IRS-1), a substrate for the activated insulin receptor tyrosine kinase, may account for the multiple functions of insulin. Recent studies have shown that activation of the insulin receptor leads to the regulation of focal adhesion proteins, such as a dephosphorylation of focal adhesion kinase (pp125FAK). We show here that C-terminal Src kinase (Csk), which phosphorylates C-terminal tyrosine residues of Src fam

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Volberg, Tova, Lewis Romer, Eli Zamir, and Benjamin Geiger. "pp60c-src and related tyrosine kinases: a role in the assembly and reorganization of matrix adhesions." Journal of Cell Science 114, no. 12 (2001): 2279–89. http://dx.doi.org/10.1242/jcs.114.12.2279.

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Activation of tyrosine kinases during integrin-mediated cell-matrix adhesion is involved both in the regulation of focal contact assembly and in the initiation of signaling processes at the cell-matrix adhesive interface. In order to determine the role of pp60c-src and related kinases in these processes, we have compared the dynamic reorganization of phosphotyrosine, vinculin, focal adhesion kinase and tensin in cells with altered expression of Src-family kinases. Both null cells for pp60c-src and triple knockout cells for pp60c-src, pp59fyn, and pp62c-yes exhibited decreased phosphotyrosine l

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Du, Quan-Sheng, Xiu-Rong Ren, Yi Xie, Qiang Wang, Lin Mei, and Wen-Cheng Xiong. "Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK." Journal of Cell Science 114, no. 16 (2001): 2977–87. http://dx.doi.org/10.1242/jcs.114.16.2977.

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Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2) are structurally related tyrosine kinases. They are implicated in regulating actin cytoskeleton organization, a process critical for cell migration, mitosis and tumor metastasis. In this paper, we demonstrate that, although both PYK2 and FAK were expressed and colocalized at focal adhesions in fibroblasts,microinjection of PYK2, but not FAK, in Swiss 3T3 fibroblastic cells led to reorganization of focal adhesions and cell rounding. PYK2-mediated actin cytoskeleton reorganization required the PYK2 N terminus, the focal adhesi

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Cobb, B. S., M. D. Schaller, T. H. Leu, and J. T. Parsons. "Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK." Molecular and Cellular Biology 14, no. 1 (1994): 147–55. http://dx.doi.org/10.1128/mcb.14.1.147.

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Changes in cellular growth and dramatic alterations in cell morphology and adhesion are common features of cells transformed by oncogenic protein tyrosine kinases, such as pp60src and other members of the Src family. In this report, we present evidence for the stable association of two Src family kinases (pp60src and pp59fyn) with tyrosine-phosphorylated forms of a focal adhesion-associated protein tyrosine kinase, pp125FAK. In Src-transformed chicken embryo cells, most of the pp125FAK was stably complexed with activated pp60src (e.g., pp60(527F). The stable association of pp125FAK with pp60(5

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Cobb, B. S., M. D. Schaller, T. H. Leu, and J. T. Parsons. "Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK." Molecular and Cellular Biology 14, no. 1 (1994): 147–55. http://dx.doi.org/10.1128/mcb.14.1.147-155.1994.

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Changes in cellular growth and dramatic alterations in cell morphology and adhesion are common features of cells transformed by oncogenic protein tyrosine kinases, such as pp60src and other members of the Src family. In this report, we present evidence for the stable association of two Src family kinases (pp60src and pp59fyn) with tyrosine-phosphorylated forms of a focal adhesion-associated protein tyrosine kinase, pp125FAK. In Src-transformed chicken embryo cells, most of the pp125FAK was stably complexed with activated pp60src (e.g., pp60(527F). The stable association of pp125FAK with pp60(5

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Eleniste, Pierre P., and Angela Bruzzaniti. "Focal Adhesion Kinases in Adhesion Structures and Disease." Journal of Signal Transduction 2012 (July 19, 2012): 1–12. http://dx.doi.org/10.1155/2012/296450.

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Cell adhesion to the extracellular matrix (ECM) is essential for cell migration, proliferation, and embryonic development. Cells can contact the ECM through a wide range of matrix contact structures such as focal adhesions, podosomes, and invadopodia. Although they are different in structural design and basic function, they share common remodeling proteins such as integrins, talin, paxillin, and the tyrosine kinases FAK, Pyk2, and Src. In this paper, we compare and contrast the basic organization and role of focal adhesions, podosomes, and invadopodia in different cells. In addition, we discus

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Li, J., H. Avraham, RA Rogers, S. Raja, and S. Avraham. "Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakaryocytes." Blood 88, no. 2 (1996): 417–28. http://dx.doi.org/10.1182/blood.v88.2.417.bloodjournal882417.

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We have recently isolated a cDNA encoding a novel human intracellular tyrosine kinase, termed RAFTK (for a related adhesion focal tyrosine kinase). The RAFTK cDNA, which encodes a polypeptide of 1,009 amino acids, shares 65% homology to the focal adhesion kinase (FAK), including several consensus motifs. In this report, we describe the biochemical characterization and functional analysis of the RAFTK protein. Coexpression of RAFTK and FAK proteins in megakaryocytic cells and blood platelets was observed. Using a specific antibody to RAFTK and the monoclonal antibody 2A7 to FAK, FAK and RAFTK c

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Garcia, Joe G. N., Kane L. Schaphorst, Alexander D. Verin, Suryanarayana Vepa, Carolyn E. Patterson, and Viswanathan Natarajan. "Diperoxovanadate alters endothelial cell focal contacts and barrier function: role of tyrosine phosphorylation." Journal of Applied Physiology 89, no. 6 (2000): 2333–43. http://dx.doi.org/10.1152/jappl.2000.89.6.2333.

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Diperoxovanadate (DPV), a potent tyrosine kinase activator and protein tyrosine phosphatase inhibitor, was utilized to explore bovine pulmonary artery endothelial cell barrier regulation. DPV produced dose-dependent decreases in transendothelial electrical resistance (TER) and increases in permeability to albumin, which were preceded by brief increases in TER (peak TER effect at 10–15 min). The significant and sustained DPV-mediated TER reductions were primarily the result of decreased intercellular resistance, rather than decreased resistance between the cell and the extracellular matrix, and

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Hildebrand, J. D., M. D. Schaller, and J. T. Parsons. "Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase." Molecular Biology of the Cell 6, no. 6 (1995): 637–47. http://dx.doi.org/10.1091/mbc.6.6.637.

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Focal adhesion kinase (pp125FAK or FAK) and paxillin colocalize with integrins in structures called focal adhesions. pp125FAK plays an important role in the transmission of integrin-induced cytoplasmic signals. Paxillin has also been implicated in cell signaling by virtue of its association with the protein tyrosine kinases pp60src and Csk (C-terminal Src kinase) as well as with the adapter/oncoprotein p47gag-crk. In this report we show that endogenous pp125FAK and paxillin form a stable complex both in vivo and in vitro and that this interaction is direct, requiring only pp125FAK and paxillin

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Dissertations / Theses on the topic "Focal Adhesion Protein-Tyrosine Kinases"

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Pylayeva, Yuliya. "Role of focal adhesion kinase in mammary gland tumorigenesis /." Access full-text from WCMC, 2008. http://proquest.umi.com/pqdweb?did=1528351831&sid=1&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Easley, Charles Allen. "Fibronectin-dependent activation of CaMK-II promotes focal adhesion disassembly by inducing tyrosine dephosphorylation of FAK and paxillin /." Unavailable until 8/19/2013, 2008. http://hdl.handle.net/10156/2272.

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Hamadi, Abdelkader Rondé Philippe. "Rôle de FAK (Focal Adhesion Kinase) dans le turnover des points d'adhérence durant la migration cellulaire." Strasbourg : Université Louis Pasteur, 2008. http://eprints-scd-ulp.u-strasbg.fr:8080/1011/01/HAMADI_Abdelkader3_2008.pdf.

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Bailey, Kelly M. "Focal adhesion kinase mediates caveolin-1 expression during epithelial to mesenchymal transition a novel pathway regulating aspects of cell motility in cancer /." Morgantown, W. Va. : [West Virginia University Libraries], 2008. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5804.

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Thesis (Ph. D.)--West Virginia University, 2008.<br>Title from document title page. Document formatted into pages; contains x, 229 p. : ill. (some col.). Includes abstract. Includes bibliographical references.

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Cao, Yangxiezi. "A chemical-biology approach for screening novel inhibitors of focal adhesion signaling in relation to breast cancer /." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111572.

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Focal adhesion kinase (FAK), a non-receptor kinase, is a key regulator of integrin and focal adhesion signaling required for cancer cell survival, cell migration, and cell invasion. Amplification/Overexpression of FAK occurs in a wide variety of human cancers, supporting a role in carcinogenesis. Moreover, preclinical studies using cancer models where FAK is genetically inhibited indicate that this kinase is a potential therapeutic target to interfere with cancer progression. However, very little progress has been made in the identification of chemical inhibitors for potential therapeutic appl

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Hamadi, Abdelkader. "Rôle de FAK (Focal Adhesion Kinase) dans le turnover des points d’adhérence durant la migration cellulaire." Université Louis Pasteur (Strasbourg) (1971-2008), 2008. https://publication-theses.unistra.fr/public/theses_doctorat/2008/HAMADI_Abdelkader_2008.pdf.

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Antunes, João Eustáquio 1971. "Novas quinazolinas 2,4,8-dissubstituídas com potencial atividade de inibição da quinase de adesão focal (FAK)." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/310204.

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Orientador : Kleber Gomes Franchini<br>Tese (Doutorado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas<br>Made available in DSpace on 2018-08-22T00:30:15Z (GMT). No. of bitstreams: 1 Antunes_JoaoEustaquio_D.pdf: 5472161 bytes, checksum: d84f6389e6baf3e2959126f6345e6a14 (MD5) Previous issue date: 2013<br>Resumo: A compreensão de como a quinase de adesão focal (FAK) contribui para os processos de hipertrofia, insuficiência cardíaca e câncer são de grande interesse científico. Um dos nossos objetivos específicos é desenvolver inibidores desta tirosina quinase com vistas à su

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Cordeiro, Isabelle Bezerra 1983. "Estudos proteômicos revelam um novo papel da proteína FAK na regulação do splicing do mRNA." [s.n.], 2014. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314412.

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Orientador: Kleber Gomes Franchini<br>Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia<br>Made available in DSpace on 2018-08-25T14:22:48Z (GMT). No. of bitstreams: 1 Cordeiro_IsabelleBezerra_D.pdf: 17466566 bytes, checksum: de71f83d2b4d3c8e0f0269f5d61d332d (MD5) Previous issue date: 2014<br>Resumo: A proteína Focal Adhesion Kinase (FAK; PTK2) participa de vários processos celulares. A identificação das proteínas parceiras de FAK tem contribuído para o entendimento de suas múltiplas funções celulares. Utilizando um sistema de indução de FAK fusionada a uma cauda de

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Fouquet, Baptiste. "Etude fonctionnelle de l'interaction de la phosphoprotéine du virus de la rage avec la protéine cellulaire FAK (Focal Adhésion Kinase)." Paris 7, 2012. http://www.theses.fr/2012PA077116.

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Le virus de la rage est un virus à ARN simple brin de polarité négative codant pour 5 protéines virales dont la protéine P, le cofacteur de la polymérase. Un crible double hybride avec la protéine P a permis l'identification d'un partenaire cellulaire, la protéine FAK, qui constitue les complexes d'adhérence et est impliquée dans la régulation de différents processus cellulaires (survie, migration et cycle cellulaire). Nous avons confirmé l'interaction entre les 2 protéines par co-immunoprécipitation et colocalisation en microscopie confocale. Après avoir identifié que le domaine FRNK de FAK i

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Annerén, Cecilia. "The Tyrosine Kinase GTK : Signal Transduction and Biological Function." Doctoral thesis, Uppsala University, Department of Medical Cell Biology, 2001. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1384.

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<p>Protein tyrosine kinases play an important role in the regulation of various cellular processes such as</p><p>growth, differentiation and survival. GTK, a novel SRC-like cytoplasmic tyrosine kinase, was recently cloned from a mouse insulinoma cell line and the present work was conducted in order to find a biological function of GTK in insulin producing and neuronal cells. It was observed that kinase active GTK-mutants, expressed in RINm5F cells, transferred to the cell nucleus and increased the levels of the cell cycle regulatory protein p27<sup>KIP1</sup>, reduced cell growth and stimulate

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Book chapters on the topic "Focal Adhesion Protein-Tyrosine Kinases"

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Chichger, Havovi, Katie L. Grinnell, and Elizabeth O. Harrington. "Protein Kinase C Isoforms in the Formation of Focal Adhesion Complexes: Investigated by Cell Impedance." In Electric Cell-Substrate Impedance Sensing and Cancer Metastasis. Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4927-6_2.

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Conference papers on the topic "Focal Adhesion Protein-Tyrosine Kinases"

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Hirt, Ulrich A., Juergen Braunger, Michael Schleicher, et al. "Abstract A249: BI 853520, a potent and highly selective inhibitor of protein tyrosine kinase 2 (focal adhesion kinase), shows efficacy in multiple xenograft models of human cancer." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-a249.

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Kemmis, Carly M., and Diane R. Wagner. "FAK, SMAD and MAPK Pathways Diverge During Osteogenic and Chondrogenic Differentiation of Adipose-Derived Mesenchymal Cells." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206474.

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Adipose-derived mesenchymal cells (AMCs) are a promising cell source for orthopaedic tissue engineering applications due to their accessibility and multi-lineage potential [1]. However, future use in bone and cartilage regeneration requires a comprehensive understanding of the pathways driving AMCs to osteogenic and chondrogenic lineages. We have previously demonstrated the dual function of a single medium containing bone morphogenetic protein-6 (BMP-6) on differentiation of AMCs; in the presence of BMP-6, monolayer culture induces osteogenic differentiation while pellet culture stimulates cho

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Crompton, Brian, Anne Carlton, Jinyan Du, Andrew Kung, and Kimberly Stegmaier. "Abstract 1613: High-throughput tyrosine kinase activity profiling identifies focal adhesion kinase (FAK) as a new target in Ewing sarcoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1613.

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Kurenova, Elena V., Darrell Hunt, Deniz Ucar, et al. "Abstract C137: Pinpointing a protein‐protein interaction site of focal adhesion kinase and VEGFR‐3 suppresses cancer growthin vivo." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-c137.

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Kemeny, Steven F., and Alisa Morss Clyne. "High Glucose Alters Endothelial Cell Response to Shear Stress." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206531.

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Endothelial cells line the walls of all blood vessels, where they maintain homeostasis through control of vascular tone, permeability, inflammation, and the growth and regression of blood vessels. Endothelial cells are mechanosensitive to fluid shear stress, elongating and aligning in the flow direction [1–2]. This shape change is driven by rearrangement of the actin cytoskeleton and focal adhesions [2]. Hyperglycemia, a hallmark of diabetes, affects endothelial cell function. High glucose has been shown to increase protein kinase C, formation of glucose-derived advanced glycation end-products

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El-Kurdi, Mohammed S., J. Scott Van Epps, Robert J. Toth, et al. "Regulation of Cell Adhesion and De-Adhesion Proteins in Veins Perfused Under Arterial Conditions Ex-Vivo." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-61531.

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Failure of veins employed as arterial bypass grafts via intimal hyperplasia (IH) often occurs within 5 years after implantation, requiring re-operation in 60% of all cases1. IH is characterized by de-adhesion, followed by migration of medial and adventitial smooth muscle cells (SMCs) and myofibroblasts into the intima, where they demonstrate uncontrolled proliferation. It is thought that this process may be induced by the abrupt exposure of the veins to the dynamic mechanical environment of the arterial circulation2. Veins are much thinner walled and more distensible than arteries. Therefore,

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Ye, Jianfeng, Baoguo Chen, and Lisa X. Xu. "Shear Stress Effect on the Production of Nitric Oxide in Cultured Rat Aorta Endothelial Cells." In ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-33074.

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Atherosclerotic lesions tend to develop in regions where there are separations from unidirectional laminar blood flow, typically near branches, bifurcations, regions of arterial narrowing, and curvatures in the arteries (1, 2). Obviously, homodynamic forces play a key role in atherosclerosis. Studies also indicate that vascular endothelium function disturbance, especially impairment of endothelium dependent vasodilation, is involved (3). Shear stress affects endothelial cells in many ways, such as cytoskeletal rearrangement, decrease of intracellular pH, release of PGI2 and some growth factors

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