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

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Published: 4 June 2021

Last updated: 6 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Vuori, K., H. Hirai, S. Aizawa, and E. Ruoslahti. "Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases." Molecular and Cellular Biology 16, no. 6 (1996): 2606–13. http://dx.doi.org/10.1128/mcb.16.6.2606.

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Integrin-mediated cell adhesion triggers intracellular signaling cascades, including tyrosine phosphorylation of intracellular proteins. Among these are the focal adhesion proteins p130cas (Cas) and focal adhesion kinase (FAK). Here we identify the kinase(s) mediating integrin-induced Cas phosphorylation and characterize protein-protein interactions mediated by phosphorylated Cas. We found that expression of a constitutively active FAK in fibroblasts results in a consecutive tyrosine phosphorylation of Cas. This effect required the autophosphorylation site of FAK, which is a binding site for S

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12

Schaller, Michael D., Jeffrey D. Hildebrand, and J. Thomas Parsons. "Complex Formation with Focal Adhesion Kinase: A Mechanism to Regulate Activity and Subcellular Localization of Src Kinases." Molecular Biology of the Cell 10, no. 10 (1999): 3489–505. http://dx.doi.org/10.1091/mbc.10.10.3489.

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Tyrosine phosphorylation of focal adhesion kinase (FAK) creates a high-affinity binding site for the src homology 2 domain of the Src family of tyrosine kinases. Assembly of a complex between FAK and Src kinases may serve to regulate the subcellular localization and the enzymatic activity of members of the Src family of kinases. We show that simultaneous overexpression of FAK and pp60c-srcor p59fynresults in the enhancement of the tyrosine phosphorylation of a limited number of cellular substrates, including paxillin. Under these conditions, tyrosine phosphorylation of paxillin is largely cell

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13

Sun, Yongjun, You Chen, Liying Zhan, Linan Zhang, Jie Hu, and Zibin Gao. "The role of non-receptor protein tyrosine kinases in the excitotoxicity induced by the overactivation of NMDA receptors." Reviews in the Neurosciences 27, no. 3 (2016): 283–89. http://dx.doi.org/10.1515/revneuro-2015-0037.

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AbstractProtein tyrosine phosphorylation is one of the primary modes of regulation of N-methyl-d-aspartate (NMDA) receptors. The non-receptor tyrosine kinases are one of the two types of protein tyrosine kinases that are involved in this process. The overactivation of NMDA receptors is a primary reason for neuron death following cerebral ischemia. Many studies have illustrated the important role of non-receptor tyrosine kinases in ischemia insults. This review introduces the roles of Src, Fyn, focal adhesion kinase, and proline-rich tyrosine kinase 2 in the excitotoxicity induced by the overac

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14

Angers-Loustau, Alexandre, Jean-François Côté, and Michel L. Tremblay. "Roles of protein tyrosine phosphatases in cell migration and adhesion." Biochemistry and Cell Biology 77, no. 6 (1999): 493–505. http://dx.doi.org/10.1139/o99-064.

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Signal transduction pathways are often seen as cascades of kinases, whereas phosphatases are relinquished to the housekeeping function of resetting the individual elements to a resting state. However, critical biological processes such as cellular migration require a coordinated and constant remodeling of the actin cytoskeleton as well as a rapid turnover of the cell-substratum linkages that necessitate the concomitant action of antagonistic enzymes. Tyrosine phosphorylation was long known to be involved in adhesion and de-adhesion mediated via the integrin receptors. As the roles of tyrosine

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15

Moszczynska, Anna, and Michal Opas. "Regulation of adhesion-related protein tyrosine kinases during in vitro differentiation of retinal pigment epithelial cells: translocation of pp60c-src to the nucleus is accompanied by downregulation of pp125FAK." Biochemistry and Cell Biology 72, no. 1-2 (1994): 43–48. http://dx.doi.org/10.1139/o94-007.

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In the present report we show that induction of expression of a differentiated phenotype in cultured retinal pigmented epithelium of chick embryo is accompanied by coordinate regulation of expression and distribution of two adhesion-related nonreceptor protein tyrosine kinases, pp60c-src and pp125FAK∙pp60c-src translocates from the cell surface in flat undifferentiated cells to the nucleus in the packed differentiated cells. In contrast, pp125FAK, abundant in focal adhesions of flat undifferentiated cells, is downregulated in cells that have differentiated and packed into an epithelial sheet.K

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16

Xiong, W. C., M. Macklem, and J. T. Parsons. "Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein." Journal of Cell Science 111, no. 14 (1998): 1981–91. http://dx.doi.org/10.1242/jcs.111.14.1981.

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Focal adhesion kinase and the recently identified proline-rich tyrosine kinase 2 (PYK2), also known as cell adhesion kinase β, related adhesion focal tyrosine kinase or calcium-dependent protein tyrosine kinase, define a new family of non-receptor protein tyrosine kinases. Activation of PYK2 has been implicated in multiple signaling events, including modulation of ion channels, T- and B-cell receptor signaling and cell death. Mechanisms underlying the functional diversity of PYK2 are unclear. Here, we provide evidence for two novel alternatively expressed isoforms of PYK2. One isoform, designa

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17

Hildebrand, J. D., J. M. Taylor, and J. T. Parsons. "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase." Molecular and Cellular Biology 16, no. 6 (1996): 3169–78. http://dx.doi.org/10.1128/mcb.16.6.3169.

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The integrin family of cell surface receptors mediates cell adhesion to components of the extracellular matrix (ECM). Integrin engagement with the ECM initiates signaling cascades that regulate the organization of the actin-cytoskeleton and changes in gene expression. The Rho subfamily of Ras-related low-molecular-weight GTP-binding proteins and several protein tyrosine kinases have been implicated in mediating various aspects of integrin-dependent alterations in cell homeostasis. Focal adhesion kinase (FAK or pp125FAK) is one of the tyrosine kinases predicted to be a critical component of int

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18

Taniyama, Yoshihiro, David S. Weber, Petra Rocic, et al. "Pyk2- and Src-Dependent Tyrosine Phosphorylation of PDK1 Regulates Focal Adhesions." Molecular and Cellular Biology 23, no. 22 (2003): 8019–29. http://dx.doi.org/10.1128/mcb.23.22.8019-8029.2003.

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ABSTRACT 3-Phosphoinositide-dependent protein kinase 1 (PDK1) is a signal integrator that activates the AGC superfamily of serine/threonine kinases. PDK1 is phosphorylated on tyrosine by oxidants, although its regulation by agonists that stimulate G-protein-coupled receptor signaling pathways and the physiological consequences of tyrosine phosphorylation in this setting have not been fully identified. We found that angiotensin II stimulates the tyrosine phosphorylation of PDK1 in vascular smooth muscle in a calcium- and c-Src-dependent manner. The calcium-activated tyrosine kinase Pyk2 acts as

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19

Schaller, M. D., J. D. Hildebrand, J. D. Shannon, J. W. Fox, R. R. Vines, and J. T. Parsons. "Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src." Molecular and Cellular Biology 14, no. 3 (1994): 1680–88. http://dx.doi.org/10.1128/mcb.14.3.1680.

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The phosphorylation of protein tyrosine kinases (PTKs) on tyrosine residues is a critical regulatory event that modulates catalytic activity and triggers the physical association of PTKs with Src homology 2 (SH2)-containing proteins. The integrin-linked focal adhesion kinase, pp125FAK, exhibits extracellular matrix-dependent phosphorylation on tyrosine and physically associates with two nonreceptor PTKs, pp60src and pp59fyn, via their SH2 domains. Herein, we identify Tyr-397 as the major site of tyrosine phosphorylation on pp125FAK both in vivo and in vitro. Tyrosine 397 is located at the junc

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20

Schaller, M. D., J. D. Hildebrand, J. D. Shannon, J. W. Fox, R. R. Vines, and J. T. Parsons. "Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src." Molecular and Cellular Biology 14, no. 3 (1994): 1680–88. http://dx.doi.org/10.1128/mcb.14.3.1680-1688.1994.

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The phosphorylation of protein tyrosine kinases (PTKs) on tyrosine residues is a critical regulatory event that modulates catalytic activity and triggers the physical association of PTKs with Src homology 2 (SH2)-containing proteins. The integrin-linked focal adhesion kinase, pp125FAK, exhibits extracellular matrix-dependent phosphorylation on tyrosine and physically associates with two nonreceptor PTKs, pp60src and pp59fyn, via their SH2 domains. Herein, we identify Tyr-397 as the major site of tyrosine phosphorylation on pp125FAK both in vivo and in vitro. Tyrosine 397 is located at the junc

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21

Fuortes, M., W. W. Jin, and C. Nathan. "Beta 2 integrin-dependent tyrosine phosphorylation of paxillin in human neutrophils treated with tumor necrosis factor." Journal of Cell Biology 127, no. 5 (1994): 1477–83. http://dx.doi.org/10.1083/jcb.127.5.1477.

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The focal adhesion protein paxillin undergoes tyrosine phosphorylation in response to signals mediated by integrins, neuropeptides and oncogene products, possibly via activation of the focal adhesion-associated kinase, p125FAK. In the present work, tumor necrosis factor-alpha (TNF) stimulated tyrosine phosphorylation of paxillin in human neutrophils. Cell adhesion and participation of the beta 2 integrin CD18 were necessary, but not sufficient, for the response. Adherent neutrophils also tyrosine phosphorylated paxillin in response to phorbol ester, formylmethionyl-leucyl-phenylalanine and ops

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22

Woods, A., and J. R. Couchman. "Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component." Molecular Biology of the Cell 5, no. 2 (1994): 183–92. http://dx.doi.org/10.1091/mbc.5.2.183.

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Focal adhesion formation in fibroblasts results from complex transmembrane signaling processes initiated by extracellular matrix molecules. Although a role for integrins with attendant tyrosine kinases has been established, there is evidence that cell surface heparan sulfate proteoglycans (HSPGs) are also involved with an associated role of protein kinase C. The identity of the proteoglycan has remained elusive, but we now report that syndecan 4 (ryudocan/amphiglycan) is present in focal adhesions of a number of cell types. Affinity-purified antibodies raised against a unique portion of the cy

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23

Chrzanowska-Wodnicka, M., and K. Burridge. "Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation." Journal of Cell Science 107, no. 12 (1994): 3643–54. http://dx.doi.org/10.1242/jcs.107.12.3643.

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Tyrosine phosphorylation is known to regulate the formation of focal adhesions in cells adhering to extracellular matrix (ECM). We have investigated the possible involvement of tyrosine phosphorylation and the focal adhesion kinase (FAK) in the cytoskeletal changes induced by serum or lysophosphatidic acid (LPA) in quiescent Swiss 3T3 fibroblasts. As shown previously by others, quiescent cells stimulated with serum or LPA reveal a rapid reappearance of focal adhesions and stress fibers. Here we show that this is accompanied by an increase in phosphotyrosine in focal adhesions and specifically

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24

Hassid, Aviv, Shile Huang, and Jian Yao. "Role of PTP-1B in aortic smooth muscle cell motility and tyrosine phosphorylation of focal adhesion proteins." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 1 (1999): H192—H198. http://dx.doi.org/10.1152/ajpheart.1999.277.1.h192.

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Recent studies have focused attention on the role of protein tyrosine kinases in vascular smooth muscle cell biology, but similar information regarding protein tyrosine phosphatases (PTP) is sparse. PTP-1B is a ubiquitous nonreceptor phosphatase with uncertain function and substrates that are mostly unidentified. We used antisense oligodeoxynucleotides (ODN) against PTP-1B to investigate the role of endogenous PTP-1B in motility of primary cultures of rat aortic smooth muscle cells (RASMC). Antisense ODN decreased PTP-1B protein levels and activity in a concentration-dependent fashion, whereas

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25

Zhang, Zheng, Hava Avraham, and David M. Cohen. "Urea and NaCl differentially regulate FAK and RAFTK/PYK2 in mIMCD3 renal medullary cells." American Journal of Physiology-Renal Physiology 275, no. 3 (1998): F447—F451. http://dx.doi.org/10.1152/ajprenal.1998.275.3.f447.

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Two cytosolic tyrosine kinases, focal adhesion kinase (FAK) and the newly described FAK homolog, related adhesion focal tyrosine kinase (RAFTK, also called PYK2 and CAKβ), have been implicated in signaling to multiple mitogen-activated protein kinase (MAPK) pathways. Therefore, the ability of NaCl and urea to activate these kinases was investigated by in vitro kinase assay and anti-phosphotyrosine immunoblotting. RAFTK was promptly but only transiently activated by urea (within 1 min; 45%), whereas NaCl activated this kinase at 1, 5, 15, and 30 min of treatment (35–60%). In contrast, FAK exhib

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26

Eide, B. L., C. W. Turck, and J. A. Escobedo. "Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK." Molecular and Cellular Biology 15, no. 5 (1995): 2819–27. http://dx.doi.org/10.1128/mcb.15.5.2819.

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A number of cellular processes, such as proliferation, differentiation, and transformation, are regulated by cell-extracellular matrix interactions. Previous studies have identified a novel tyrosine kinase, the focal adhesion kinase p125FAK, as a component of cell adhesion plaques. p125FAK was identified as a 125-kDa tyrosine-phosphorylated protein in cells transformed by the v-src oncogene. p125FAK is an intracellular protein composed of three domains: a central domain with homology to protein tyrosine kinases, flanked by two noncatalytic domains of 400 amino acids which bear no significant h

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27

Gilmore, A. P., and L. H. Romer. "Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation." Molecular Biology of the Cell 7, no. 8 (1996): 1209–24. http://dx.doi.org/10.1091/mbc.7.8.1209.

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It has been proposed that the focal adhesion kinase (FAK) mediates focal adhesion formation through tyrosine phosphorylation during cell adhesion. We investigated the role of FAK in focal adhesion structure and function. Loading cells with a glutathione-S-transferase fusion protein (GST-Cterm) containing the FAK focal adhesion targeting sequence, but not the kinase domain, decreased the association of endogenous FAK with focal adhesions. This displacement of endogenous FAK in both BALB/c 3T3 cells and human umbilical vein endothelial cells loaded with GST-Cterm decreased focal adhesion phospho

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28

Gonzalez-Fernandez, L., B. Macias-Garcia, S. C. Loux, D. D. Varner, and K. Hinrichs. "Focal Adhesion Kinases and Calcium/Calmodulin-Dependent Protein Kinases Regulate Protein Tyrosine Phosphorylation in Stallion Sperm." Biology of Reproduction 88, no. 6 (2013): 138. http://dx.doi.org/10.1095/biolreprod.112.107078.

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Wang, Jian-Feng, In-Woo Park та Jerome E. Groopman. "Stromal cell-derived factor-1α stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood 95, № 8 (2000): 2505–13. http://dx.doi.org/10.1182/blood.v95.8.2505.

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Abstract The stromal cell-derived factor-1 (SDF-1) is an alpha chemokine that binds to the CXCR4 receptor. Knock-out studies in mice demonstrate that this ligand-receptor pair is essential in hematopoiesis. One function of SDF-1 appears to be the regulation of migration of hematopoietic progenitor cells. We previously characterized signal transduction pathways induced by SDF-1 in human hematopoietic progenitors and found tyrosine phosphorylation of focal adhesion components, including the related adhesion focal tyrosine kinase (RAFTK), the adaptor molecule p130 Cas, and the cytoskeletal prote

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30

Wang, Jian-Feng, In-Woo Park та Jerome E. Groopman. "Stromal cell-derived factor-1α stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood 95, № 8 (2000): 2505–13. http://dx.doi.org/10.1182/blood.v95.8.2505.008k24_2505_2513.

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The stromal cell-derived factor-1 (SDF-1) is an alpha chemokine that binds to the CXCR4 receptor. Knock-out studies in mice demonstrate that this ligand-receptor pair is essential in hematopoiesis. One function of SDF-1 appears to be the regulation of migration of hematopoietic progenitor cells. We previously characterized signal transduction pathways induced by SDF-1 in human hematopoietic progenitors and found tyrosine phosphorylation of focal adhesion components, including the related adhesion focal tyrosine kinase (RAFTK), the adaptor molecule p130 Cas, and the cytoskeletal protein paxill

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Murphy-Ullrich, J. E., M. A. Pallero, N. Boerth, J. A. Greenwood, T. M. Lincoln, and T. L. Cornwell. "Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly." Journal of Cell Science 109, no. 10 (1996): 2499–508. http://dx.doi.org/10.1242/jcs.109.10.2499.

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Focal adhesions are specialized regions of cell membranes that are foci for the transmission of signals between the outside and the inside of the cell. Intracellular signaling events are important in the organization and stability of these structures. In previous work, we showed that the counter-adhesive extracellular matrix proteins, thrombospondin, tenascin, and SPARC, induce the disassembly of focal adhesion plaques and we identified the active regions of these proteins. In order to determine the mechanisms whereby the anti-adhesive matrix proteins modulate cytoskeletal organization and foc

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Canobbio, Ilaria, Paolo Lova, Fabiola Sinigaglia, Cesare Balduini, and Mauro Torti. "Proline-rich Tyrosine Kinase 2 and Focal Adhesion Kinase Are Involved in Different Phases of Platelet Activation by vWF." Thrombosis and Haemostasis 87, no. 03 (2002): 509–17. http://dx.doi.org/10.1055/s-0037-1613032.

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SummaryStimulation of human platelets with von Willebrand factor (vWF) induces the rapid tyrosine phosphorylation of several proteins, but very little is known on the tyrosine kinases involved in this process. In the present work, we investigated and compared the activation of two related tyrosine kinases expressed in platelets: the proline-rich tyrosine kinase 2 (Pyk2) and the focal adhesion kinase (FAK). Both kinases were tyrosine phosphorylated upon vWF interaction with glycoprotein Ib-IX-V complex, but with different mechanisms. Tyrosine phosphorylation of FAK was totally dependent on thro

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Hildebrand, J. D., M. D. Schaller, and J. T. Parsons. "Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions." Journal of Cell Biology 123, no. 4 (1993): 993–1005. http://dx.doi.org/10.1083/jcb.123.4.993.

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The integrin family of heterodimeric cell surface receptors play critical roles in multiple biological processes by mediating cellular adhesion to the extracellular matrix (ECM). Adhesion triggers intracellular signaling cascades, including tyrosine phosphorylation and elevation of [Ca2+]i. The Focal Adhesion Kinase (FAK or pp125FAK), a protein tyrosine kinase that colocalizes with integrins in cellular focal adhesions, is a prime candidate for a mediator of integrin signaling events. Here we report an analysis of the domain structure of FAK in which we have identified a contiguous stretch of

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Woods, A., and J. R. Couchman. "Protein kinase C involvement in focal adhesion formation." Journal of Cell Science 101, no. 2 (1992): 277–90. http://dx.doi.org/10.1242/jcs.101.2.277.

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Matrix molecules such as fibronectin can promote cell attachment, spreading and focal adhesion formation. Although some interactions of fibronectin with cell surface receptors have now been identified, the consequent activation of intracellular messenger systems by cell/matrix interactions have still to be elucidated. We show here that the kinase inhibitors H7 and HA1004 reduce focal adhesion and stress fiber formation in response to fibronectin in a dose-dependent manner, and that activators of protein kinase C can promote their formation under conditions where they do not normally form. Fibr

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Stoker, Andrew W. "Protein tyrosine phosphatases and signalling." Journal of Endocrinology 185, no. 1 (2005): 19–33. http://dx.doi.org/10.1677/joe.1.06069.

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A cornerstone of many cell-signalling events rests on reversible phosphorylation of tyrosine residues on proteins. The reversibility relies on the coordinated actions of protein tyrosine kinases and protein tyrosine phosphatases (PTPs), both of which exist as large protein families. This review focuses on the rapidly evolving field of the PTPs. We now know that rather than simply scavenging phosphotyrosine, the PTPs specifically regulate a wide range of signalling pathways. To illustrate this and to highlight current areas of agreement and contention in the field, this review will present our

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Yamboliev, Ilia A., Jennifer Chen, and William T. Gerthoffer. "PI 3-kinases and Src kinases regulate spreading and migration of cultured VSMCs." American Journal of Physiology-Cell Physiology 281, no. 2 (2001): C709—C718. http://dx.doi.org/10.1152/ajpcell.2001.281.2.c709.

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Pulmonary artery smooth muscle cell (PASMC) adhesion, spreading, and migration depend on matrix-stimulated reorganization of focal adhesions. Platelet-derived growth factor (PDGF) activates intracellular signal transduction cascades that also regulate adhesion, spreading, and migration, but the signaling molecules involved in these events are poorly defined. We hypothesized that phosphatidylinositol (PI) 3-kinases and Src tyrosine kinases translate matrix and PDGF-initiated signals into cell motility. In experiments with cultured canine PASMCs, inhibition of PI 3-kinases with wortmannin (0.3 μ

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Lin, Tsung H., Andrew E. Aplin, Yu Shen, et al. "Integrin-mediated Activation of MAP Kinase Is Independent of FAK: Evidence for Dual Integrin Signaling Pathways in Fibroblasts." Journal of Cell Biology 136, no. 6 (1997): 1385–95. http://dx.doi.org/10.1083/jcb.136.6.1385.

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Integrin-mediated cell adhesion causes activation of MAP kinases and increased tyrosine phosphorylation of focal adhesion kinase (FAK). Autophosphorylation of FAK leads to the binding of SH2-domain proteins including Src-family kinases and the Grb2–Sos complex. Since Grb2–Sos is a key regulator of the Ras signal transduction pathway, one plausible hypothesis has been that integrin-mediated tyrosine phosphorylation of FAK leads to activation of the Ras cascade and ultimately to mitogen activated protein (MAP) kinase activation. Thus, in this scenario FAK would serve as an upstream regulator of

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Schaller, Michael D., and J. Thomas Parsons. "Focal adhesion kinase: an integrin-linked protein tyrosine kinase." Trends in Cell Biology 3, no. 8 (1993): 258–62. http://dx.doi.org/10.1016/0962-8924(93)90053-4.

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Zhang, Zhiyong, Gonzalo Izaguirre, Siang-Yo Lin, Hwa Young Lee, Erik Schaefer, and Beatrice Haimovich. "The Phosphorylation of Vinculin on Tyrosine Residues 100 and 1065, Mediated by Src Kinases, Affects Cell Spreading." Molecular Biology of the Cell 15, no. 9 (2004): 4234–47. http://dx.doi.org/10.1091/mbc.e04-03-0264.

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Vinculin is a conserved actin binding protein localized in focal adhesions and cell-cell junctions. Here, we report that vinculin is tyrosine phosphorylated in platelets spread on fibrinogen and that the phosphorylation is Src kinases dependent. The phosphorylation of vinculin on tyrosine was reconstituted in vanadate treated COS-7 cells coexpressing c-Src. The tyrosine phosphorylation sites in vinculin were mapped to residues 100 and 1065. A phosphorylation-specific antibody directed against tyrosine residue 1065 reacted with phosphorylated platelet vinculin but failed to react with vinculin

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Brown, M. C., J. A. Perrotta, and C. E. Turner. "Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding." Journal of Cell Biology 135, no. 4 (1996): 1109–23. http://dx.doi.org/10.1083/jcb.135.4.1109.

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Paxillin is a 68-kD focal adhesion phosphoprotein that interacts with several proteins including members of the src family of tyrosine kinases, the transforming protein v-crk, and the cytoskeletal proteins vinculin and the tyrosine kinase, focal adhesion kinase (FAK). This suggests a function for paxillin as a molecular adaptor, responsible for the recruitment of structural and signaling molecules to focal adhesions. The current study defines the vinculin- and FAK-interaction domains on paxillin and identifies the principal paxillin focal adhesion targeting motif. Using truncation and deletion

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Li, Xiong, Ruth C. Dy, William G. Cance, Lee M. Graves, and H. Shelton Earp. "Interactions between Two Cytoskeleton-associated Tyrosine Kinases: Calcium-dependent Tyrosine Kinase and Focal Adhesion Tyrosine Kinase." Journal of Biological Chemistry 274, no. 13 (1999): 8917–24. http://dx.doi.org/10.1074/jbc.274.13.8917.

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Vomastek, Tomas, Marcin P. Iwanicki, Hans-Joerg Schaeffer, Adel Tarcsafalvi, J. Thomas Parsons, and Michael J. Weber. "RACK1 Targets the Extracellular Signal-Regulated Kinase/Mitogen-Activated Protein Kinase Pathway To Link Integrin Engagement with Focal Adhesion Disassembly and Cell Motility." Molecular and Cellular Biology 27, no. 23 (2007): 8296–305. http://dx.doi.org/10.1128/mcb.00598-07.

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ABSTRACT The extracellular signal-regulated kinase (ERK) cascade is activated in response to a multitude of extracellular signals and converts these signals into a variety of specific biological responses, including cell differentiation, cell movement, cell division, and apoptosis. The specificity of the biological response is likely to be controlled in large measure by the localization of signaling, thus enabling ERK activity to be directed towards specific targets. Here we show that the RACK1 scaffold protein functions specifically in integrin-mediated activation of the mitogen-activated pro

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KABIR, Jahangir, Melvin LOBO, and Ian ZACHARY. "Staurosporine induces endothelial cell apoptosis via focal adhesion kinase dephosphorylation and focal adhesion disassembly independent of focal adhesion kinase proteolysis." Biochemical Journal 367, no. 1 (2002): 145–55. http://dx.doi.org/10.1042/bj20020665.

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The survival of endothelial cells is dependent on interactions between the matrix and integrins mediated through focal adhesions. Focal adhesion kinase (FAK) is thought to play a key role in maintaining focal adhesion function and cell survival, whereas caspase-mediated FAK proteolysis is implicated in focal adhesion disassembly during apoptosis. We examined the relationship between changes in FAK phosphorylation and proteolysis during apoptosis of primary porcine aortic endothelial cells (PAEC) induced by staurosporine, a widely used apoptogenic agent in diverse cell types. Staurosporine-indu

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Arregui, Carlos O., Janne Balsamo, and Jack Lilien. "Impaired Integrin-mediated Adhesion and Signaling in Fibroblasts Expressing a Dominant-negative Mutant PTP1B." Journal of Cell Biology 143, no. 3 (1998): 861–73. http://dx.doi.org/10.1083/jcb.143.3.861.

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To investigate the role of nonreceptor protein tyrosine phosphatase 1B (PTP1B) in β1-integrin– mediated adhesion and signaling, we transfected mouse L cells with normal and catalytically inactive forms of the phosphatase. Parental cells and cells expressing the wild-type or mutant PTP1B were assayed for (a) adhesion, (b) spreading, (c) presence of focal adhesions and stress fibers, and (d) tyrosine phosphorylation. Parental cells and cells expressing wild-type PTP1B show similar morphology, are able to attach and spread on fibronectin, and form focal adhesions and stress fibers. In contrast, c

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Schaller, M. D., C. A. Borgman, and J. T. Parsons. "Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK." Molecular and Cellular Biology 13, no. 2 (1993): 785–91. http://dx.doi.org/10.1128/mcb.13.2.785.

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Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction pathway. Here we report the isolation of cDNAs encoding the C-terminal, noncatalytic domain of the FAK kinase, termed FRNK (FAK-related nonkinase). Both the FAK- and FRNK-encoded polypeptides, pp125FAK and p41/p43FRNK, are expressed in normal chic

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Schaller, M. D., C. A. Borgman, and J. T. Parsons. "Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK." Molecular and Cellular Biology 13, no. 2 (1993): 785–91. http://dx.doi.org/10.1128/mcb.13.2.785-791.1993.

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Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction pathway. Here we report the isolation of cDNAs encoding the C-terminal, noncatalytic domain of the FAK kinase, termed FRNK (FAK-related nonkinase). Both the FAK- and FRNK-encoded polypeptides, pp125FAK and p41/p43FRNK, are expressed in normal chic

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Lee, Sang Yoon, Sergey Voronov, Kresimir Letinic, Angus C. Nairn, Gilbert Di Paolo та Pietro De Camilli. "Regulation of the interaction between PIPKIγ and talin by proline-directed protein kinases". Journal of Cell Biology 168, № 5 (2005): 789–99. http://dx.doi.org/10.1083/jcb.200409028.

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The interaction of talin with phosphatidylinositol(4) phosphate 5 kinase type Iγ (PIPKIγ) regulates PI(4,5)P2 synthesis at synapses and at focal adhesions. Here, we show that phosphorylation of serine 650 (S650) within the talin-binding sequence of human PIPKIγ blocks this interaction. At synapses, S650 is phosphorylated by p35/Cdk5 and mitogen-activated protein kinase at rest, and dephosphorylated by calcineurin upon stimulation. S650 is also a substrate for cyclin B1/Cdk1 and its phosphorylation in mitosis correlates with focal adhesion disassembly. Phosphorylation by Src of the tyrosine adj

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Chang, Fumin, Christopher A. Lemmon, Dongeun Park та Lewis H. Romer. "FAK Potentiates Rac1 Activation and Localization to Matrix Adhesion Sites: A Role for βPIX". Molecular Biology of the Cell 18, № 1 (2007): 253–64. http://dx.doi.org/10.1091/mbc.e06-03-0207.

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FAK, a cytoplasmic protein tyrosine kinase, is activated and localized to focal adhesions upon cell attachment to extracellular matrix. FAK null cells spread poorly and exhibit altered focal adhesion turnover. Rac1 is a member of the Rho-family GTPases that promotes membrane ruffling, leading edge extension, and cell spreading. We investigated the activation and subcellular location of Rac1 in FAK null and FAK reexpressing fibroblasts. FAK reexpressers had a more robust pattern of Rac1 activation after cell adhesion to fibronectin than the FAK null cells. Translocation of Rac1 to focal adhesio

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de Virgilio, Maddalena, William B. Kiosses та Sanford J. Shattil. "Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells". Journal of Cell Biology 165, № 3 (2004): 305–11. http://dx.doi.org/10.1083/jcb.200402064.

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Stable platelet aggregation, adhesion, and spreading during hemostasis are promoted by outside-in αIIbβ3 signals that feature rapid activation of c-Src and Syk, delayed activation of FAK, and cytoskeletal reorganization. To evaluate these αIIbβ3–tyrosine kinase interactions at nanometer proximity in living cells, we monitored bioluminescence resonance energy transfer between GFP and Renilla luciferase chimeras and bimolecular fluorescence complementation between YFP half-molecule chimeras. These techniques revealed that αIIbβ3 interacts with c-Src at the periphery of nonadherent CHO cells. Aft

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Schaller, M. D., C. A. Otey, J. D. Hildebrand, and J. T. Parsons. "Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains." Journal of Cell Biology 130, no. 5 (1995): 1181–87. http://dx.doi.org/10.1083/jcb.130.5.1181.

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The integrins have recently been implicated in signal transduction. A likely mediator of integrin signaling is focal adhesion kinase (pp125FAK or FAK), a structurally distinct protein tyrosine kinase that becomes enzymatically activated upon engagement of integrins with their ligands. A second candidate signaling molecule is paxillin, a focal adhesion associated, cytoskeletal protein that coordinately becomes phosphorylated on tyrosine upon activation of pp125FAK. Paxillin physically complexes with two protein tyrosine kinases, pp60src and Csk (COOH-terminal src kinase), and the oncoprotein p4

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