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Journal articles on the topic 'Protein Kinase, c-Src'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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1

Brábek, J., D. Mojžita, L. Hamplová, and Petr Folk. "The Regulatory Region of Prague C v-Src Inhibits the Activity of the Schmidt-Ruppin A v-Src Kinase Domain." Folia Biologica 48, no. 1 (2002): 28–33. https://doi.org/10.14712/fb2002048010028.

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Existing variants of the oncogene v-src differ in their transforming potential as well as in the range of their hosts. We compared the protein kinase activities of two Prague C v-Src variants (PRC and H19), reported to be of low oncogenic potential (Plachý et al., 1995), with the highly oncogenic Schmidt-Ruppin A v-Src (SRA). We employed in vitro kinase assays of affinity-purified proteins expressed in rabbit reticulocyte lysate and in S. cerevisiae. In both systems used, the specific kinase activity of the Prague C v-Sre kinases amounted to only ca 20% of the activity of SRA. This positions t

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2

Sabe, H., M. Okada, H. Nakagawa, and H. Hanafusa. "Activation of c-Src in cells bearing v-Crk and its suppression by Csk." Molecular and Cellular Biology 12, no. 10 (1992): 4706–13. http://dx.doi.org/10.1128/mcb.12.10.4706-4713.1992.

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The protein product of the CT10 virus, p47gag-crk (v-Crk), which contains Src homology region 2 (SH2) and 3 (SH3) domains but lacks a kinase domain, is believed to cause an increase in cellular protein tyrosine phosphorylation. A candidate tyrosine kinase, Csk (C-terminal Src kinase), has been implicated in c-Src Tyr-527 phosphorylation, which negatively regulates the protein tyrosine kinase of pp60c-src (c-Src). To investigate how c-Src kinase activity is regulated in vivo, we first looked at whether v-Crk can activate c-Src kinase. We found that cooverexpression of v-Crk and c-Src caused ele

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3

Sabe, H., M. Okada, H. Nakagawa, and H. Hanafusa. "Activation of c-Src in cells bearing v-Crk and its suppression by Csk." Molecular and Cellular Biology 12, no. 10 (1992): 4706–13. http://dx.doi.org/10.1128/mcb.12.10.4706.

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The protein product of the CT10 virus, p47gag-crk (v-Crk), which contains Src homology region 2 (SH2) and 3 (SH3) domains but lacks a kinase domain, is believed to cause an increase in cellular protein tyrosine phosphorylation. A candidate tyrosine kinase, Csk (C-terminal Src kinase), has been implicated in c-Src Tyr-527 phosphorylation, which negatively regulates the protein tyrosine kinase of pp60c-src (c-Src). To investigate how c-Src kinase activity is regulated in vivo, we first looked at whether v-Crk can activate c-Src kinase. We found that cooverexpression of v-Crk and c-Src caused ele

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4

Brott, B. K., S. Decker, M. C. O'Brien, and R. Jove. "Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein." Molecular and Cellular Biology 11, no. 10 (1991): 5059–67. http://dx.doi.org/10.1128/mcb.11.10.5059-5067.1991.

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GTPase-activating protein (GAP) enhances the rate of GTP hydrolysis by cellular Ras proteins and is implicated in mitogenic signal transduction. GAP is phosphorylated on tyrosine in cells transformed by Rous sarcoma virus and serves as an in vitro substrate of the viral Src (v-Src) kinase. Our previous studies showed that GAP complexes stably with normal cellular Src (c-Src), although its association with v-Src is less stable. To further investigate the molecular basis for interactions between GAP and the Src kinases, we examined GAP association with and phosphorylation by a series of c-Src an

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5

Brott, B. K., S. Decker, M. C. O'Brien, and R. Jove. "Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein." Molecular and Cellular Biology 11, no. 10 (1991): 5059–67. http://dx.doi.org/10.1128/mcb.11.10.5059.

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GTPase-activating protein (GAP) enhances the rate of GTP hydrolysis by cellular Ras proteins and is implicated in mitogenic signal transduction. GAP is phosphorylated on tyrosine in cells transformed by Rous sarcoma virus and serves as an in vitro substrate of the viral Src (v-Src) kinase. Our previous studies showed that GAP complexes stably with normal cellular Src (c-Src), although its association with v-Src is less stable. To further investigate the molecular basis for interactions between GAP and the Src kinases, we examined GAP association with and phosphorylation by a series of c-Src an

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6

Klomp, Jennifer E., Vincent Huyot, Anne-Marie Ray, Kerrie B. Collins, Asrar B. Malik, and Andrei V. Karginov. "Mimicking transient activation of protein kinases in living cells." Proceedings of the National Academy of Sciences 113, no. 52 (2016): 14976–81. http://dx.doi.org/10.1073/pnas.1609675114.

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Physiological stimuli activate protein kinases for finite periods of time, which is critical for specific biological outcomes. Mimicking this transient biological activity of kinases is challenging due to the limitations of existing methods. Here, we report a strategy enabling transient kinase activation in living cells. Using two protein-engineering approaches, we achieve independent control of kinase activation and inactivation. We show successful regulation of tyrosine kinase c-Src (Src) and Ser/Thr kinase p38α (p38), demonstrating broad applicability of the method. By activating Src for fi

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7

Zhang, Jiayi, Ching-hang Wong, Weiliang Xia та ін. "Regulation of Sertoli-Germ Cell Adherens Junction Dynamics via Changes in Protein-Protein Interactions of the N-Cadherin-β-Catenin Protein Complex which Are Possibly Mediated by c-Src and Myotubularin-Related Protein 2: An in Vivo Study Using an Androgen Suppression Model". Endocrinology 146, № 3 (2005): 1268–84. http://dx.doi.org/10.1210/en.2004-1194.

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Using a well characterized model of cell-cell actin-based adherens junction (AJ) disruption by suppressing the intratesticular testosterone level in adult rats with testosterone-estradiol implants, we have confirmed earlier findings that Sertoli-germ cell AJ dynamics are regulated by the activation of kinases via putative signaling pathways but with some unexpected findings as follows. First, the loss of germ cells from the seminiferous epithelium during androgen suppression was associated with a surge in myotubularin-related protein 2 (MTMR2, a lipid phosphatase, in which adult MTMR2−/− mice

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8

Richard, S., D. Yu, K. J. Blumer, et al. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1." Molecular and Cellular Biology 15, no. 1 (1995): 186–97. http://dx.doi.org/10.1128/mcb.15.1.186.

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src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21ras GTPase-activating protein, as a src family kinase SH3-domain-bi

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9

Ahn, Bong-Hyun, Shi Yeon Kim, Eun Hee Kim, et al. "Transmodulation between Phospholipase D and c-Src Enhances Cell Proliferation." Molecular and Cellular Biology 23, no. 9 (2003): 3103–15. http://dx.doi.org/10.1128/mcb.23.9.3103-3115.2003.

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ABSTRACT Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src syner

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10

Levy, J. B., and J. S. Brugge. "Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts." Molecular and Cellular Biology 9, no. 8 (1989): 3332–41. http://dx.doi.org/10.1128/mcb.9.8.3332-3341.1989.

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The c-src protein isolated from neuronal cells (pp60c-src+) displays a higher level of protein kinase activity than does pp60c-src from nonneural tissues. There are two structural alterations present in the amino-terminal half of pp60c-src+ expressed in neurons which could contribute to the enhanced activity of this form of pp60c-src: (i) a hexapeptide insert located at amino acid 114 of avian pp60c-src+ and (ii) a novel site(s) of serine phosphorylation. We characterized pp60c-src+ expressed in a nonneuronal cell type to identify factors that regulate the activity of the c-src+ protein and th

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11

Levy, J. B., and J. S. Brugge. "Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts." Molecular and Cellular Biology 9, no. 8 (1989): 3332–41. http://dx.doi.org/10.1128/mcb.9.8.3332.

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The c-src protein isolated from neuronal cells (pp60c-src+) displays a higher level of protein kinase activity than does pp60c-src from nonneural tissues. There are two structural alterations present in the amino-terminal half of pp60c-src+ expressed in neurons which could contribute to the enhanced activity of this form of pp60c-src: (i) a hexapeptide insert located at amino acid 114 of avian pp60c-src+ and (ii) a novel site(s) of serine phosphorylation. We characterized pp60c-src+ expressed in a nonneuronal cell type to identify factors that regulate the activity of the c-src+ protein and th

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12

Wang, Y. H., F. Li, J. H. Schwartz, P. J. Flint, and S. C. Borkan. "c-Src and HSP72 interact in ATP-depleted renal epithelial cells." American Journal of Physiology-Cell Physiology 281, no. 5 (2001): C1667—C1675. http://dx.doi.org/10.1152/ajpcell.2001.281.5.c1667.

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Disruption of cell contact sites during ischemia contributes to the loss of organ function in acute renal failure. Because prior heat stress protects cell contact sites in ATP-depleted renal epithelial cells in vitro, we hypothesized that heat shock protein 72 (HSP72), the major inducible cytoprotectant in mammalian cells, interacts with protein kinases that regulate cell-cell and cell-matrix interactions. ATP depletion increased the content of Tyr416 Src, the activated form of this kinase. c-Src activation was associated with an increase in the tyrosine phosphorylation state of β-catenin, pax

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13

Yan, S. R., M. Huang, and G. Berton. "Signaling by adhesion in human neutrophils: activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen." Journal of Immunology 158, no. 4 (1997): 1902–10. http://dx.doi.org/10.4049/jimmunol.158.4.1902.

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Abstract Src family kinases are implicated in signaling by integrins in polymorphonuclear neutrophils (PMN). To identify proteins present in complexes with Src family kinases, we subjected p58(c-fgr) or p53/56(lyn) immunoprecipitates from Triton X-100 lysates of PMN incubated on fibrinogen-coated surfaces to in vitro kinase assays. Assays on p58(c-fgr) or p53/56(lyn) immunoprecipitates from Triton lysates of PMN induced to spread over fibrinogen in response to TNF-alpha showed that several proteins form complexes with Src family kinases and can be phosphorylated in vitro. Immunoblot analysis s

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14

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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15

Zhao, Y., H. Uyttendaele, J. G. Krueger, M. Sudol, and H. Hanafusa. "Inactivation of c-Yes tyrosine kinase by elevation of intracellular calcium levels." Molecular and Cellular Biology 13, no. 12 (1993): 7507–14. http://dx.doi.org/10.1128/mcb.13.12.7507-7514.1993.

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We have previously shown that the c-Src tyrosine kinase is activated four- to fivefold when cultured keratinocytes differentiate following the elevation of intracellular calcium levels. In contrast to c-Src, another Src family tyrosine kinase, c-Yes, was rapidly inactivated in these same cells, despite its marked similarity in structure and enzymatic activity to c-Src. The inactivation of c-Yes was independent of the protein kinase C pathway, which is usually activated by elevation of intracellular calcium levels. The protein levels of c-Src and c-Yes were not altered, but the phosphotyrosine

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16

Zhao, Y., H. Uyttendaele, J. G. Krueger, M. Sudol, and H. Hanafusa. "Inactivation of c-Yes tyrosine kinase by elevation of intracellular calcium levels." Molecular and Cellular Biology 13, no. 12 (1993): 7507–14. http://dx.doi.org/10.1128/mcb.13.12.7507.

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We have previously shown that the c-Src tyrosine kinase is activated four- to fivefold when cultured keratinocytes differentiate following the elevation of intracellular calcium levels. In contrast to c-Src, another Src family tyrosine kinase, c-Yes, was rapidly inactivated in these same cells, despite its marked similarity in structure and enzymatic activity to c-Src. The inactivation of c-Yes was independent of the protein kinase C pathway, which is usually activated by elevation of intracellular calcium levels. The protein levels of c-Src and c-Yes were not altered, but the phosphotyrosine

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17

Nemeth, S. P., L. G. Fox, M. DeMarco, and J. S. Brugge. "Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein." Molecular and Cellular Biology 9, no. 3 (1989): 1109–19. http://dx.doi.org/10.1128/mcb.9.3.1109-1119.1989.

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To examine how amino acid sequences outside of the catalytic domain of pp60c-src influence the functional activity of this protein, we have introduced deletion mutations within the amino-terminal half of pp60c-src. These mutations caused distinct changes in the biochemical properties of the c-src gene products and in the properties of cells infected with retroviruses carrying these mutant c-src genes. Cells expressing the c-srcNX protein, which contains a deletion of amino acids 15 to 89, displayed a refractile, spindle-shaped morphology, formed intermediate-sized, tightly packed colonies in s

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18

Nemeth, S. P., L. G. Fox, M. DeMarco, and J. S. Brugge. "Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein." Molecular and Cellular Biology 9, no. 3 (1989): 1109–19. http://dx.doi.org/10.1128/mcb.9.3.1109.

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To examine how amino acid sequences outside of the catalytic domain of pp60c-src influence the functional activity of this protein, we have introduced deletion mutations within the amino-terminal half of pp60c-src. These mutations caused distinct changes in the biochemical properties of the c-src gene products and in the properties of cells infected with retroviruses carrying these mutant c-src genes. Cells expressing the c-srcNX protein, which contains a deletion of amino acids 15 to 89, displayed a refractile, spindle-shaped morphology, formed intermediate-sized, tightly packed colonies in s

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19

Patwardhan, Parag, and Marilyn D. Resh. "Myristoylation and Membrane Binding Regulate c-Src Stability and Kinase Activity." Molecular and Cellular Biology 30, no. 17 (2010): 4094–107. http://dx.doi.org/10.1128/mcb.00246-10.

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ABSTRACT Myristoylation is critical for membrane association of Src kinases, but a role for myristate in regulating other aspects of Src biology has not been explored. In the c-Abl tyrosine kinase, myristate binds within a hydrophobic pocket at the base of the kinase domain and latches the protein into an autoinhibitory conformation. A similar pocket has been predicted to exist in c-Src, raising the possibility that Src might also be regulated by myristoylation. Here we show that in contrast to the case for c-Abl, myristoylation exerts a positive effect on c-Src kinase activity. We also demons

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20

Stanczyk, Haley, Carolina Galeano-Naranjo, and Tianyan Gao. "Abstract 4144: PTPTF negatively regulates c-Src kinase through the dephosphorylation of the activation loop." Cancer Research 85, no. 8_Supplement_1 (2025): 4144. https://doi.org/10.1158/1538-7445.am2025-4144.

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Kinases and phosphatases play a dynamic role in the regulation of signaling propagation. c-Src is an oncogenic kinase that plays multifunctional roles in the initiation and progression of many cancers, including breast, colorectal and lung cancers. The activity of c-Src kinase is tightly regulated by the phosphorylation status of two key tyrosine residues (Tyr419 and Tyr530 in human c-Src) that controls its propensity for entering an active conformation. Phosphorylation of Tyr530 at the C-terminus of c-Src locks the kinase in an inactive confirmation whereas phosphorylation of Tyr419 in the ac

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21

Burnham, Mary Rose, Pamela J. Bruce-Staskal, Mary T. Harte, et al. "Regulation of c-SRC Activity and Function by the Adapter Protein CAS." Molecular and Cellular Biology 20, no. 16 (2000): 5865–78. http://dx.doi.org/10.1128/mcb.20.16.5865-5878.2000.

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ABSTRACT SRC family kinases play essential roles in a variety of cellular functions, including proliferation, survival, differentiation, and apoptosis. The activities of these kinases are regulated by intramolecular interactions and by heterologous binding partners that modulate the transition between active and inactive structural conformations. p130 CAS (CAS) binds directly to both the SH2 and SH3 domains of c-SRC and therefore has the potential to structurally alter and activate this kinase. In this report, we demonstrate that overexpression of full-length CAS in COS-1 cells induces c-SRC-d

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22

Mukhopadhyay, Chandrani, Aleata Triplett, Tom Bargar, Carol Heckman, Kay-Uwe Wagner, and Mayumi Naramura. "Casitas B-cell lymphoma (Cbl) proteins protect mammary epithelial cells from proteotoxicity of active c-Src accumulation." Proceedings of the National Academy of Sciences 113, no. 51 (2016): E8228—E8237. http://dx.doi.org/10.1073/pnas.1615677113.

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Casitas B-cell lymphoma (Cbl) family ubiquitin ligases negatively regulate tyrosine kinase-dependent signal transduction by promoting degradation of active kinases. We and others previously reported that loss of Cbl functions caused hyperproliferation in lymphoid and hematopoietic systems. Unexpectedly, Cbl deletion in Cbl-b–null, Cbl-c–null primary mouse mammary epithelial cells (MECs) (Cbl triple-deficiency) induced rapid cell death despite enhanced MAP kinase and AKT activation. Acute Cbl triple-deficiency elicited distinct transcriptional and biochemical responses with partial overlap with

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23

Adolph, Dörte, Nadine Flach, Katharina Mueller, Dirk H. Ostareck, and Antje Ostareck-Lederer. "Deciphering the Cross Talk between hnRNP K and c-Src: the c-Src Activation Domain in hnRNP K Is Distinct from a Second Interaction Site." Molecular and Cellular Biology 27, no. 5 (2006): 1758–70. http://dx.doi.org/10.1128/mcb.02014-06.

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ABSTRACT The protein tyrosine kinase c-Src is regulated by two intramolecular interactions. The repressed state is achieved through the interaction of the Src homology 2 (SH2) domain with the phosphorylated C-terminal tail and the association of the SH3 domain with a polyproline type II helix formed by the linker region between SH2 and the kinase domain. hnRNP K, the founding member of the KH domain protein family, is involved in chromatin remodeling, regulation of transcription, and translation of specific mRNAs and is a target in different signal transduction pathways. In particular, it func

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24

Cunningham-Smith, K. A., R. Witherdin, L. Hetherington, M. A. Baker, and R. Aitken. "277.The role of pp60c-src tyrosine kinase in sperm capacitation." Reproduction, Fertility and Development 16, no. 9 (2004): 277. http://dx.doi.org/10.1071/srb04abs277.

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A protein kinase A-dependent tyrosine phosphorylation pathway in mammalian spermatozoa has been demonstrated to exist, and is unique to this cell type. As PKA is incapable of directly phosphorylating substrates on tyrosine residues, much research has focused on the identification of an intermediary tyrosine kinase which can be activated by serine/threonine phosphorylation via PKA. Inhibitory studies using genistein, tryphostin, erbstatin and herbimycin A, have demonstrated that the src family of kinases may be responsible for the tyrosine phosphorylation events seen during capacitation (1). Al

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Yin, Guoyong, Judith Haendeler, Chen Yan, and Bradford C. Berk. "GIT1 Functions as a Scaffold for MEK1-Extracellular Signal-Regulated Kinase 1 and 2 Activation by Angiotensin II and Epidermal Growth Factor." Molecular and Cellular Biology 24, no. 2 (2004): 875–85. http://dx.doi.org/10.1128/mcb.24.2.875-885.2004.

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ABSTRACT Activation of the mitogen-activated protein kinase pathway represented by extracellular signal-regulated kinases (ERK1/2) and activation of the upstream kinase (MEK1) are critical events for growth factor signal transduction. c-Src has been proposed as a common mediator for these signals in response to both G protein-coupled receptors (GPCRs) and tyrosine kinase-coupled receptors (TKRs). Here we show that the GPCR kinase-interacting protein 1 (GIT1) is a substrate for c-Src that associates with MEK1 in vascular smooth-muscle cells and human embryonic kidney 293 cells. GIT1 binding via

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26

Villalobo, Antonio. "Ca2+ Signaling and Src Functions in Tumor Cells." Biomolecules 13, no. 12 (2023): 1739. http://dx.doi.org/10.3390/biom13121739.

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Signaling by calcium ion (Ca2+) plays a prominent role in cell physiology, and these mechanisms are frequently altered in tumor cells. In this review, we consider the interplay of Ca2+ signaling and the functions of the proto-oncogene non-receptor tyrosine kinase c-Src in tumor cells, and the viral oncogenic variant v-Src in transformed cells. Also, other members of the Src-family kinases are considered in this context. The role of Ca2+ in the cell is frequently mediated by Ca2+-binding proteins, where the Ca2+-sensor protein calmodulin (CaM) plays a prominent, essential role in many cellular

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27

Boschelli, F., S. M. Uptain, and J. J. Lightbody. "The lethality of p60v-src in Saccharomyces cerevisiae and the activation of p34CDC28 kinase are dependent on the integrity of the SH2 domain." Journal of Cell Science 105, no. 2 (1993): 519–28. http://dx.doi.org/10.1242/jcs.105.2.519.

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The lethal effects of the expression of the oncogenic protein tyrosine kinase p60v-src in Saccharomyces cerevisiae are associated with a loss of cell cycle control at the G1/S and G2/M checkpoints. Results described here indicate that the ability of v-Src to kill yeast is dependent on the integrity of the SH2 domain, a region of the Src protein involved in recognition of proteins phosphorylated on tyrosine. Catalytically active v-Src proteins with deletions in the SH2 domain have little effect on yeast growth, unlike wild-type v-Src protein, which causes accumulation of large-budded cells, per

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Salinas-Garcia, M. Carmen, Marina Plaza-Garrido, and Ana Camara-Artigas. "The impact of oncogenic mutations of the viral Src kinase on the structure and stability of the SH3 domain." Acta Crystallographica Section D Structural Biology 77, no. 6 (2021): 854–66. http://dx.doi.org/10.1107/s2059798321004344.

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Src kinase belongs to the family of Src-related nonreceptor tyrosine kinases. Because of its physiological role in cell growth and proliferation, its activity is strictly controlled by several mechanisms. Nevertheless, in viral Src kinase (v-Src) some of these mechanisms fail, and its uncontrolled activity is responsible for the occurrence of cancer. Here, the crystal structures of three SH3-domain mutants of v-Src were determined to unveil the effects of these oncogenic mutations in this regulatory domain. Mutations in the n-Src and distal loops have a low impact on the overall structure of t

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Amatya, Neha, David Yin-wei Lin, and Amy H. Andreotti. "Dynamic regulatory features of the protein tyrosine kinases." Biochemical Society Transactions 47, no. 4 (2019): 1101–16. http://dx.doi.org/10.1042/bst20180590.

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Abstract The SRC, Abelson murine leukemia viral oncogene homolog 1, TEC and C-terminal SRC Kinase families of non-receptor tyrosine kinases (collectively the Src module kinases) mediate an array of cellular signaling processes and are therapeutic targets in many disease states. Crystal structures of Src modules kinases provide valuable insights into the regulatory mechanisms that control activation and generate a framework from which drug discovery can advance. The conformational ensembles visited by these multidomain kinases in solution are also key features of the regulatory machinery contro

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Dobkin-Bekman, Masha, Michal Naidich, Liat Rahamim та ін. "A Preformed Signaling Complex Mediates GnRH-Activated ERK Phosphorylation of Paxillin and FAK at Focal Adhesions in LβT2 Gonadotrope Cells". Molecular Endocrinology 23, № 11 (2009): 1850–64. http://dx.doi.org/10.1210/me.2008-0260.

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Abstract Most receptor tyrosine kinases and G protein-coupled receptors (GPCRs) operate via a limited number of MAPK cascades but still exert diverse functions, and therefore signal specificity remains an enigma. Also, most GPCR ligands utilize families of receptors for mediation of diverse biological actions; however, the mammalian type I GnRH receptor (GnRHR) seems to be the sole receptor mediating GnRH-induced gonadotropin synthesis and release. Signaling complexes associated with GPCRs may thus provide the means for signal specificity. Here we describe a signaling complex associated with t

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Gentili, Claudia, Ricardo Boland та Ana Russo de Boland. "Implication of Gβγ proteins and c-SRC tyrosine kinase in parathyroid hormone-induced signal transduction in rat enterocytes". Journal of Endocrinology 188, № 1 (2006): 69–78. http://dx.doi.org/10.1677/joe.1.06397.

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Parathyroid hormone (PTH) interacts in target tissues with a G protein-coupled receptor (GPCR) localized in the plasma membrane. Although activation of GPCR can elicit rapid stimulation of cellular protein tyrosine phosphorylation, the mechanism by which G proteins activate protein-tyrosine kinases is not completely understood. In the present work, we demonstrate that PTH rapidly increases the activity of non-receptor tyrosine kinase c-Src in rat intestinal cells (enterocytes). The response is biphasic, the early phase is fast and transient, peaking at 30 s (+120%), while the second phase prog

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32

Wang, H. C., and R. L. Erikson. "Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases." Molecular Biology of the Cell 3, no. 12 (1992): 1329–37. http://dx.doi.org/10.1091/mbc.3.12.1329.

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We have used myelin basic protein immobilized in sodium dodecyl sulfate-polyacrylamide gels to identify protein kinases after gel electrophoresis, followed by protein kinase reactions. This technique has permitted us to detect three protein kinases in serum-deprived cells transformed by p60src. On induction of cellular transformation by a temperature-sensitive v-src, a p87 protein kinase is activated within 30 min and remains activated in fully transformed cells. The p63 protein kinase is not fully activated until 24 h but remains activated in transformed cells. The commonly studied p42MBPK is

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Jha, Vibhu, Marco Macchia, Tiziano Tuccinardi, and Giulio Poli. "Three-Dimensional Interactions Analysis of the Anticancer Target c-Src Kinase with Its Inhibitors." Cancers 12, no. 8 (2020): 2327. http://dx.doi.org/10.3390/cancers12082327.

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Src family kinases (SFKs) constitute the biggest family of non-receptor tyrosine kinases considered as therapeutic targets for cancer therapy. An aberrant expression and/or activation of the proto-oncogene c-Src kinase, which is the oldest and most studied member of the family, has long been demonstrated to play a major role in the development, growth, progression and metastasis of numerous human cancers, including colon, breast, gastric, pancreatic, lung and brain carcinomas. For these reasons, the pharmacological inhibition of c-Src activity represents an effective anticancer strategy and a

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Klein, N. P., and R. J. Schneider. "Activation of Src family kinases by hepatitis B virus HBx protein and coupled signaling to Ras." Molecular and Cellular Biology 17, no. 11 (1997): 6427–36. http://dx.doi.org/10.1128/mcb.17.11.6427.

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The HBx protein of hepatitis B virus (HBV) is a small transcriptional transactivator that is essential for infection by the mammalian hepadnaviruses and is thought to be a cofactor in HBV-mediated liver cancer. HBx stimulates signal transduction pathways by acting in the cytoplasm, which accounts for many but not all of its transcriptional activities. Studies have shown that HBx protein activates Ras and downstream Ras signaling pathways including Raf, mitogen-activated protein (MAP) kinase kinase kinase (MEK), and MAP kinases. In this study, we investigated the mechanism of activation of Ras

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Bell, S. M., D. C. Connolly, N. J. Maihle, and J. L. Degen. "Differential modulation of plasminogen activator gene expression by oncogene-encoded protein tyrosine kinases." Molecular and Cellular Biology 13, no. 9 (1993): 5888–97. http://dx.doi.org/10.1128/mcb.13.9.5888-5897.1993.

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Urokinase-type plasminogen activator (uPA) gene transcription is increased > or = 50-fold in chicken embryo fibroblasts (CEF) following transformation by the protein tyrosine kinase pp60v-src. Protein phosphorylation appears to play a critical role in uPA gene expression in these cells; protein kinase C-activating phorbol esters cooperate with pp60v-src to synergistically increase uPA mRNA, whereas cyclic AMP (cAMP)-dependent protein kinase-activating agents (e.g., 8-bromo cAMP) repress uPA mRNA levels. To explore the relationship between transforming oncogenes and uPA gene expression, uPA

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Bell, S. M., D. C. Connolly, N. J. Maihle, and J. L. Degen. "Differential modulation of plasminogen activator gene expression by oncogene-encoded protein tyrosine kinases." Molecular and Cellular Biology 13, no. 9 (1993): 5888–97. http://dx.doi.org/10.1128/mcb.13.9.5888.

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Urokinase-type plasminogen activator (uPA) gene transcription is increased > or = 50-fold in chicken embryo fibroblasts (CEF) following transformation by the protein tyrosine kinase pp60v-src. Protein phosphorylation appears to play a critical role in uPA gene expression in these cells; protein kinase C-activating phorbol esters cooperate with pp60v-src to synergistically increase uPA mRNA, whereas cyclic AMP (cAMP)-dependent protein kinase-activating agents (e.g., 8-bromo cAMP) repress uPA mRNA levels. To explore the relationship between transforming oncogenes and uPA gene expression, uPA

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Shvartsman, Dmitry E., John C. Donaldson, Begoña Diaz, Orit Gutman, G. Steven Martin, and Yoav I. Henis. "Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets." Journal of Cell Biology 178, no. 4 (2007): 675–86. http://dx.doi.org/10.1083/jcb.200701133.

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Src functions depend on its association with the plasma membrane and with specific membrane-associated assemblies. Many aspects of these interactions are unclear. We investigated the functions of kinase, SH2, and SH3 domains in Src membrane interactions. We used FRAP beam-size analysis in live cells expressing a series of c-Src–GFP proteins with targeted mutations in specific domains together with biochemical experiments to determine whether the mutants can generate and bind to phosphotyrosyl proteins. Wild-type Src displays lipid-like membrane association, whereas constitutively active Src-Y5

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Auvinen, M., A. Paasinen-Sohns, H. Hirai, L. C. Andersson, and E. Hölttä. "Ornithine decarboxylase- and ras-induced cell transformations: reversal by protein tyrosine kinase inhibitors and role of pp130CAS." Molecular and Cellular Biology 15, no. 12 (1995): 6513–25. http://dx.doi.org/10.1128/mcb.15.12.6513.

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We have found that overexpression of human ornithine decarboxylase (ODC) induces cell transformation in NIH 3T3 and Rat-1 cells (M. Auvinen, A. Paasinen, L. C. Andersson, and E. Hölttä, Nature (London) 360:355-358, 1992). The ODC-transformed cells display increased levels of tyrosine phosphorylation, in particular of a cluster of 130-kDa proteins. Here we show that one of the proteins with enhanced levels of tyrosine phosphorylation in ODC-overexpressing cells is the previously described p130 substrate of pp60v-src, known to associate also with v-Crk and designated p130CAS. We also studied the

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Pertel, Thomas, Defen Zhu, Reynold A. Panettieri, Naoto Yamaguchi, Charles W. Emala, and Carol A. Hirshman. "Expression and muscarinic receptor coupling of Lyn kinase in cultured human airway smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 290, no. 3 (2006): L492—L500. http://dx.doi.org/10.1152/ajplung.00344.2005.

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Src family tyrosine kinases are signaling intermediates in a diverse array of cellular events including cell differentiation, motility, proliferation, and survival. In nonairway smooth muscle cells, muscarinic receptors directly interact with Src family tyrosine kinases. As little is known about the expression and signaling of these Src family tyrosine kinases in human airway smooth muscle cells, we determined the expression of Src family members and characterized the muscarinic receptor-mediated activation of Lyn kinase in these cells. RT-PCR revealed mRNA transcripts for FYN, c- SRC, YES, FR

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Fujii, M., D. Shalloway, and I. M. Verma. "Gene regulation by tyrosine kinases: src protein activates various promoters, including c-fos." Molecular and Cellular Biology 9, no. 6 (1989): 2493–99. http://dx.doi.org/10.1128/mcb.9.6.2493-2499.1989.

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A promoter of the nuclear proto-oncogene fos was activated by cotransfection with the viral src gene. Ability to transactivate the c-fos promoter was dependent on tyrosine kinase activity, because (i) src mutants which have reduced tyrosine kinase activity due to mutation of Tyr-416 to Phe showed lower promoter activation, (ii) pp60c-src mutants which have increased tyrosine kinase activity due to mutation of Tyr-527 to Phe also augmented c-fos promoter induction, and (iii) mutation in the ATP-binding site of pp60v-src strongly suppressed c-fos promoter activation. Tyrosine kinase activity alo

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Fujii, M., D. Shalloway, and I. M. Verma. "Gene regulation by tyrosine kinases: src protein activates various promoters, including c-fos." Molecular and Cellular Biology 9, no. 6 (1989): 2493–99. http://dx.doi.org/10.1128/mcb.9.6.2493.

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A promoter of the nuclear proto-oncogene fos was activated by cotransfection with the viral src gene. Ability to transactivate the c-fos promoter was dependent on tyrosine kinase activity, because (i) src mutants which have reduced tyrosine kinase activity due to mutation of Tyr-416 to Phe showed lower promoter activation, (ii) pp60c-src mutants which have increased tyrosine kinase activity due to mutation of Tyr-527 to Phe also augmented c-fos promoter induction, and (iii) mutation in the ATP-binding site of pp60v-src strongly suppressed c-fos promoter activation. Tyrosine kinase activity alo

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Dong, Su, Andrew Khoo, Jianxin Wei, et al. "Serum starvation regulates E-cadherin upregulation via activation of c-Src in non-small-cell lung cancer A549 cells." American Journal of Physiology-Cell Physiology 307, no. 9 (2014): C893—C899. http://dx.doi.org/10.1152/ajpcell.00132.2014.

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E-cadherin is essential for the integrity of adherens junctions between lung epithelial cells, and the loss of E-cadherin allows cell motility and is thought to promote lung cancer metastasis. While the downregulation of E-cadherin expression has been well characterized and is seen with transforming growth factor-β1 (TGF-β1) exposure, few studies have focused on E-cadherin upregulation. Here, we show that serum starvation causes increased E-cadherin expression via the activation of c-Src kinase in non-small-cell lung cancer A549 cells. Serum starvation increased E-cadherin protein levels in a

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Pleiman, C. M., M. R. Clark, L. K. Gauen, et al. "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase." Molecular and Cellular Biology 13, no. 9 (1993): 5877–87. http://dx.doi.org/10.1128/mcb.13.9.5877-5887.1993.

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Engagement of the B-cell antigen receptor complex induces immediate activation of receptor-associated Src family tyrosine kinases including p55blk, p59fyn, p53/56lyn, and perhaps p56lck, and this response is accompanied by tyrosine phosphorylation of distinct cellular substrates. These kinases act directly or indirectly to phosphorylate and/or activate effector proteins including p42 (microtubule-associated protein kinase) (MAPK), phospholipases C-gamma 1 (PLC gamma 1) and C-gamma 2 (PLC gamma 2), phosphatidylinositol 3-kinase (PI 3-K), and p21ras-GTPase-activating protein (GAP). Although coim

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Pleiman, C. M., M. R. Clark, L. K. Gauen, et al. "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase." Molecular and Cellular Biology 13, no. 9 (1993): 5877–87. http://dx.doi.org/10.1128/mcb.13.9.5877.

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Engagement of the B-cell antigen receptor complex induces immediate activation of receptor-associated Src family tyrosine kinases including p55blk, p59fyn, p53/56lyn, and perhaps p56lck, and this response is accompanied by tyrosine phosphorylation of distinct cellular substrates. These kinases act directly or indirectly to phosphorylate and/or activate effector proteins including p42 (microtubule-associated protein kinase) (MAPK), phospholipases C-gamma 1 (PLC gamma 1) and C-gamma 2 (PLC gamma 2), phosphatidylinositol 3-kinase (PI 3-K), and p21ras-GTPase-activating protein (GAP). Although coim

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45

Gout, I., R. Dhand, G. Panayotou та ін. "Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85β protein by using the baculovirus expression system". Biochemical Journal 288, № 2 (1992): 395–405. http://dx.doi.org/10.1042/bj2880395.

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PtdIns 3-kinase associates with certain activated protein-tyrosine kinase receptors and with the pp60c-src/polyoma middle-T complex, suggesting that the enzyme is involved in growth regulation. The purified PtdIns 3-kinase appears to have two subunits, of 85 kDa and 110 kDa. Structural analysis at protein and cDNA levels revealed two forms of the 85 kDa subunit, one which associates with PtdIns 3-kinase activity termed p85 alpha, and a protein of unknown function, p85 beta. Both 85 kDa proteins contain src-homology regions 2 and 3 (SH2 and SH3), but lack enzymic activity, suggesting that they

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46

Neet, K., and T. Hunter. "The nonreceptor protein-tyrosine kinase CSK complexes directly with the GTPase-activating protein-associated p62 protein in cells expressing v-Src or activated c-Src." Molecular and Cellular Biology 15, no. 9 (1995): 4908–20. http://dx.doi.org/10.1128/mcb.15.9.4908.

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CSK is a predominantly cytosolic protein-tyrosine kinase (PTK) that negatively regulates Src family PTKs by phosphorylation of a conserved tyrosine near their C termini. Little is known about how CSK itself is regulated. On the basis of immunofluorescence studies, a model has been proposed that when c-Src is activated, it is redistributed to podosomes, in which substrates become phosphorylated, creating binding sites for CSK. CSK is recruited to these sites of c-Src activation via its SH2 and SH3 domains and is then in a position to downregulate c-Src activity (B. W. Howell and J. A. Cooper, M

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Mellström, K., C. Bjelfman, U. Hammerling, and S. Påhlman. "Expression of c-src in cultured human neuroblastoma and small-cell lung carcinoma cell lines correlates with neurocrine differentiation." Molecular and Cellular Biology 7, no. 12 (1987): 4178–84. http://dx.doi.org/10.1128/mcb.7.12.4178-4184.1987.

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Human cell lines with neuronal and neuroendocrine features were examined for their expression of pp60c-src, the cellular homolog of the transforming gene product pp60v-src of Rous sarcoma virus. Four neuroblastoma (LA-N-5, SH-SY5Y, Paju, and SK-N-MC) and three small-cell lung carcinoma (U-2020, U-1690, and U-1285) cell lines were selected on the basis of their stage of neurocrine differentiation, as determined by the expression of neuron-specific enolase. In an immune complex protein kinase assay, all seven cell lines displayed c-src kinase activity which was considerably higher than that foun

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48

Mellström, K., C. Bjelfman, U. Hammerling, and S. Påhlman. "Expression of c-src in cultured human neuroblastoma and small-cell lung carcinoma cell lines correlates with neurocrine differentiation." Molecular and Cellular Biology 7, no. 12 (1987): 4178–84. http://dx.doi.org/10.1128/mcb.7.12.4178.

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Human cell lines with neuronal and neuroendocrine features were examined for their expression of pp60c-src, the cellular homolog of the transforming gene product pp60v-src of Rous sarcoma virus. Four neuroblastoma (LA-N-5, SH-SY5Y, Paju, and SK-N-MC) and three small-cell lung carcinoma (U-2020, U-1690, and U-1285) cell lines were selected on the basis of their stage of neurocrine differentiation, as determined by the expression of neuron-specific enolase. In an immune complex protein kinase assay, all seven cell lines displayed c-src kinase activity which was considerably higher than that foun

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49

Liebenhoff, U., D. Brockmeier, and P. Presek. "Substrate affinity of the protein tyrosine kinase pp60c-src is increased on thrombin stimulation of human platelets." Biochemical Journal 295, no. 1 (1993): 41–48. http://dx.doi.org/10.1042/bj2950041.

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Human blood platelets contain high levels of non-receptor protein tyrosine kinases of the Src family, particularly pp60c-src, suggesting an important role for these enzymes in platelet physiology. Indeed, in response to various agonists of platelet function, a number of proteins become phosphorylated at tyrosine residues. However, no enzymic activation of an Src-related tyrosine kinase has yet been shown in platelets. In searching for the kinase(s) responsible, we found that all agonists tested that directly or indirectly activate protein kinase C in platelets (phorbol 12-myristate, 13-acetate

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Seidel-Dugan, C., B. E. Meyer, S. M. Thomas, and J. S. Brugge. "Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src." Molecular and Cellular Biology 12, no. 4 (1992): 1835–45. http://dx.doi.org/10.1128/mcb.12.4.1835-1845.1992.

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The amino-termina, noncatalytic half of Src contains two domains, designated the Src homology 2 (SH2) and Src homology 3 (SH3) domains, that are highly conserved among members of the Src family of tyrosine kinases. The SH2 domain (which can be further divided into the B and C homology boxes) and the SH3 domain (also referred to as the A box) are also found in several proteins otherwise unrelated to protein tyrosine kinases. It is believed that these domains are important for directing specific protein-protein interactions necessary for the proper functioning of Src. To determine the importance

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