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Artículos de revistas sobre el tema "Src-family kinases (SFKs)"

Autor: Grafiati

Publicado: 11 de marzo de 2023

Última modificación: 31 de julio de 2025

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1

Wang, Jun, and Shougang Zhuang. "Src family kinases in chronic kidney disease." American Journal of Physiology-Renal Physiology 313, no. 3 (2017): F721—F728. http://dx.doi.org/10.1152/ajprenal.00141.2017.

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Src family kinases (SFKs) belong to nonreceptor protein tyrosine kinases and have been implicated in the regulation of numerous cellular processes, including cell proliferation, differentiation, migration and invasion, and angiogenesis. The role and mechanisms of SFKs in tumorgenesis have been extensively investigated, and some SFK inhibitors are currently under clinical trials for tumor treatment. Recent studies have also demonstrated the importance of SFKs in regulating the development of various fibrosis-related chronic diseases (e.g., idiopathic pulmonary fibrosis, liver fibrosis, renal fi

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2

Xiao, Xiang, Yue Yang, Baiping Mao, C. Yan Cheng, and Ya Ni. "Emerging role for SRC family kinases in junction dynamics during spermatogenesis." Reproduction 157, no. 3 (2019): R85—R94. http://dx.doi.org/10.1530/rep-18-0440.

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SRC family kinases (SFKs) are known regulators of multiple cellular events, including cell movement, differentiation, proliferation, survival and apoptosis. SFKs are expressed virtually by all mammalian cells. They are non-receptor protein kinases that phosphorylate a variety of cellular proteins on tyrosine, leading to the activation of protein targets in response to environmental stimuli. Among SFKs, SRC, YES and FYN are the ubiquitously expressed and best studied members. In fact, SRC, the prototypical SFK, was the first tyrosine kinase identified in mammalian cells. Studies have shown that

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3

Senis, Yotis A., Alexandra Mazharian, and Jun Mori. "Src family kinases: at the forefront of platelet activation." Blood 124, no. 13 (2014): 2013–24. http://dx.doi.org/10.1182/blood-2014-01-453134.

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Abstract Src family kinases (SFKs) play a central role in mediating the rapid response of platelets to vascular injury. They transmit activation signals from a diverse repertoire of platelet surface receptors, including the integrin αIIbβ3, the immunoreceptor tyrosine–based activation motif–containing collagen receptor complex GPVI-FcR γ-chain, and the von Willebrand factor receptor complex GPIb-IX-V, which are essential for thrombus growth and stability. Ligand-mediated clustering of these receptors triggers an increase in SFK activity and downstream tyrosine phosphorylation of enzymes, adapt

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4

Xiang, Binggang, Guoying Zhang, and Zhenyu Li. "Src Family Kinases Contribute to GI and Gq-Mediated Platelet Activation." Blood 118, no. 21 (2011): 5263. http://dx.doi.org/10.1182/blood.v118.21.5263.5263.

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Abstract Abstract 5263 The Src family kinases (SFKs) play an essential role in collagen- and von Willebrand factor (vWF)-mediated platelet activation. However, the role of SFKs in G protein-coupled receptor (GPCR)-mediated platelet activation is not fully understood, and little is known about the molecular mechanisms by which SFKs are activated by GPCR stimulation. Here we demonstrate that SFKs are activated by the Gq and Gi pathways, respectively and SFKs play important roles in Gq- and Gi-dependent secretion and activation. ADP induced SFK phosphorylation in wild type and Gq−/− platelets, an

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5

Evangelista, Virgilio, Zehra Pamuklar, Antonio Piccoli, et al. "Src family kinases mediate neutrophil adhesion to adherent platelets." Blood 109, no. 6 (2006): 2461–69. http://dx.doi.org/10.1182/blood-2006-06-029082.

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Abstract Polymorphonuclear leukocyte (PMN)–platelet interactions at sites of vascular damage contribute to local and systemic inflammation. We sought to determine the role of “outside-in” signaling by Src-family tyrosine kinases (SFKs) in the regulation of αMβ2-integrin–dependent PMN recruitment by activated platelets under (patho)physiologic conditions. Activation-dependent epitopes in β2 integrin were exposed at the contact sites between PMNs and platelets and were abolished by SFK inhibitors. PMNs from αMβ2−/−, hck−/−fgr−/−, and hck−/−fgr−/−lyn−/− mice had an impaired capacity to adhere wit

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6

Singh, Durgesh Kumar, Rohit Kumar Deshmukh, Praveen Kumar Narayanan, Sisinthy Shivaji, and Archana Bharadwaj Siva. "SRC family kinases in hamster spermatozoa: evidence for the presence of LCK." Reproduction 153, no. 5 (2017): 655–69. http://dx.doi.org/10.1530/rep-16-0591.

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Sperm capacitation is a prerequisite for successful fertilization. Increase in tyrosine phosphorylation is considered the hallmark of capacitation and attempts to understand its regulation are ongoing. In this regard, we attempted to study the role of SRC family kinases (SFKs) in the hamster sperm functions. Interestingly, we found the presence of the lymphocyte-specific protein tyrosine kinase, LCK, in mammalian spermatozoa and further characterized it in terms of its localization and function. LCK was found in spermatozoa of several species, and its transcript was identified in the hamster t

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7

Indovina, Paola, Iris Maria Forte, Francesca Pentimalli, and Antonio Giordano. "Targeting SRC Family Kinases in Mesothelioma: Time to Upgrade." Cancers 12, no. 7 (2020): 1866. http://dx.doi.org/10.3390/cancers12071866.

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Malignant mesothelioma (MM) is a deadly tumor mainly caused by exposure to asbestos. Unfortunately, no current treatment is able to change significantly the natural history of the disease, which has a poor prognosis in the majority of patients. The non-receptor tyrosine kinase SRC and other SRC family kinase (SFK) members are frequently hyperactivated in many cancer types, including MM. Several works have indeed suggested that SFKs underlie MM cell proliferation, survival, motility, and invasion, overall affecting multiple oncogenic pathways. Consistently, SFK inhibitors effectively counteract

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8

Bhavaraju, Kamala, Soochong Kim, and Satya P. Kunapuli. "Lyn and Fyn Kinases Positively Regulate Thromboxane Generation in Platelets." Blood 110, no. 11 (2007): 3656. http://dx.doi.org/10.1182/blood.v110.11.3656.3656.

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Abstract Src family Kinases (SFKs) are important tyrosine kinases in platelets. The family consists of 9 members (viz., Blk, Fgr, Fyn, Hck, Lck, Lyn, Src, Yes and Yrk) and many of the isoforms are expressed in platelets. SFKs are key kinases in glycoprotein (GPVI) mediated platelet activation and we have shown that these kinases play an important role in thromboxane generation. Until now, the role of specific SFKs downstream of G protein signaling in platelets is not well understood. In the present study we characterized functional roles of specific SFK members Fyn, Lyn, Lck and Src Kinases do

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9

Oneyama, Chitose, Takuya Iino, Kazunobu Saito, Kei Suzuki, Akira Ogawa, and Masato Okada. "Transforming Potential of Src Family Kinases Is Limited by the Cholesterol-Enriched Membrane Microdomain." Molecular and Cellular Biology 29, no. 24 (2009): 6462–72. http://dx.doi.org/10.1128/mcb.00941-09.

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ABSTRACT The upregulation of Src family kinases (SFKs) has been implicated in cancer progression, but the molecular mechanisms regulating their transforming potentials remain unclear. Here we show that the transforming ability of all SFK members is suppressed by being distributed to the cholesterol-enriched membrane microdomain. All SFKs could induce cell transformation when overexpressed in C-terminal Src kinase (Csk)-deficient fibroblasts. However, their transforming abilities varied depending on their affinity for the microdomain. c-Src and Blk, with a weak affinity for the microdomain due

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10

Ruiz, Ofelia S., R. Brooks Robey, Yi-Yong Qiu, et al. "Regulation of the renal Na-HCO3 cotransporter. XI. Signal transduction underlying CO2stimulation." American Journal of Physiology-Renal Physiology 277, no. 4 (1999): F580—F586. http://dx.doi.org/10.1152/ajprenal.1999.277.4.f580.

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We have previously shown that CO2 stimulation of the renal Na-HCO3 cotransporter (NBC) activity is abrogated by general inhibitors of protein tyrosine kinases. The more selective inhibitor herbimycin also blocked this effect at concentrations known to preferentially inhibit Src family kinases (SFKs). We therefore examined a role for SFKs in CO2-stimulated NBC activity. To this end, we engineered OK cells to express the COOH-terminal Src kinase (Csk), a negative regulator of SFKs. CO2 stimulated NBC activity normally in β-galactosidase-expressing and untransfected control cells. In contrast, Cs

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11

Talmor-Cohen, A., R. Tomashov-Matar, E. Eliyahu, R. Shapiro, and R. Shalgi. "Are Src family kinases involved in cell cycle resumption in rat eggs?" Reproduction 127, no. 4 (2004): 455–63. http://dx.doi.org/10.1530/rep.1.00104.

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The earliest visible indications for the transition to embryos in mammalian eggs, known as egg activation, are cortical granules exocytosis (CGE) and resumption of meiosis (RM); these events are triggered by the fertilizing spermatozoon through a series of Ca2+transients. The pathways, within the egg, leading to the intracellular Ca2+release and to the downstream cellular events, are currently under intensive investigation. The involvement of Src family kinases (SFKs) in Ca2+release at fertilization is well supported in marine invertebrate eggs but not in mammalian eggs. In a previous study we

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12

Voisset, Edwige, Fabienne Brenet, Sophie Lopez, and Paulo de Sepulveda. "SRC-Family Kinases in Acute Myeloid Leukaemia and Mastocytosis." Cancers 12, no. 7 (2020): 1996. http://dx.doi.org/10.3390/cancers12071996.

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Protein tyrosine kinases have been recognized as important actors of cell transformation and cancer progression, since their discovery as products of viral oncogenes. SRC-family kinases (SFKs) play crucial roles in normal hematopoiesis. Not surprisingly, they are hyperactivated and are essential for membrane receptor downstream signaling in hematological malignancies such as acute myeloid leukemia (AML) and mastocytosis. The precise roles of SFKs are difficult to delineate due to the number of substrates, the functional redundancy among members, and the use of tools that are not selective. Yet

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13

Sirvent, Audrey, Rudy Mevizou, Dana Naim, Marie Lafitte, and Serge Roche. "Src Family Tyrosine Kinases in Intestinal Homeostasis, Regeneration and Tumorigenesis." Cancers 12, no. 8 (2020): 2014. http://dx.doi.org/10.3390/cancers12082014.

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Src, originally identified as an oncogene, is a membrane-anchored tyrosine kinase and the Src family kinase (SFK) prototype. SFKs regulate the signalling induced by a wide range of cell surface receptors leading to epithelial cell growth and adhesion. In the intestine, the SFK members Src, Fyn and Yes regulate epithelial cell proliferation and migration during tissue regeneration and transformation, thus implicating conserved and specific functions. In patients with colon cancer, SFK activity is a marker of poor clinical prognosis and a potent driver of metastasis formation. These tumorigenic

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14

Kheilová, Kateřina, Jaroslav Petr, Tereza Žalmanová, Veronika Kučerová-Chrpová, and Dalibor Řehák. "Src family kinases are involved in the meiotic maturation of porcine oocytes." Reproduction, Fertility and Development 27, no. 7 (2015): 1097. http://dx.doi.org/10.1071/rd13352.

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Mammalian meiotic maturation is regulated by changes in the phosphorylation state of proteins involved in signalling pathways. The regulatory proteins include the family of Src tyrosine kinases. Src family kinases (SFKs) are required for meiotic maturation of mouse oocytes, and it remains to be elucidated whether they play the same role in porcine oocytes. To clarify the role of SFKs in the meiotic maturation of porcine oocytes we used inhibition of SFKs, western blotting and immunolocalisation to determine the presence of SFKs and localisation in the oocytes and assays to determine the activi

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15

Tibaldi, Elena, Andrea Venerando, Francesca Zonta, et al. "Interaction between the SH3 domain of Src family kinases and the proline-rich motif of HTLV-1 p13: a novel mechanism underlying delivery of Src family kinases to mitochondria." Biochemical Journal 439, no. 3 (2011): 505–18. http://dx.doi.org/10.1042/bj20101650.

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The association of the SH3 (Src homology 3) domain of SFKs (Src family kinases) with protein partners bearing proline-rich motifs has been implicated in the regulation of SFK activity, and has been described as a possible mechanism of relocalization of SFKs to subcellular compartments. We demonstrate in the present study for the first time that p13, an accessory protein encoded by the HTLV-1 (human T-cell leukaemia virus type 1), binds the SH3 domain of SFKs via its C-terminal proline-rich motif, forming a stable heterodimer that translocates to mitochondria by virtue of its N-terminal mitocho

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16

Donato, Nicholas J., Ji Wu, Ling-Yuan Kong, Feng Meng, Francis Lee, and Moshe Talpaz. "Constitutive Activation of SRC-Family Kinases in Chronic Myelogenous Leukemia Patients Resistant to Imatinib Mesylate in the Absence of BCR-ABL Mutations: A Rationale for Use of SRC/ABL Dual Kinase Inhibitor-Based Therapy." Blood 106, no. 11 (2005): 1087. http://dx.doi.org/10.1182/blood.v106.11.1087.1087.

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Abstract BCR-ABL is an unregulated tyrosine kinase expressed as a consequence of a reciprocal chromosomal translocation that is common in chronic myelogenous and acute lymphocytic leukemia. BCR-ABL induces transformation of hematopoetic stem cells through tyrosine phosphorylation of multiple substrates. The src-family kinases (SFKs), Lyn and Hck, are highly activated by BCR-ABL in leukemic cells and recent studies suggest that they are substrates and essential mediators of BCR-ABL signal transduction and transformation. In cells selected for resistance to the BCR-ABL inhibitor, imatinib mesyla

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17

Tamiya, Shigeo, Mansim C. Okafor, and Nicholas A. Delamere. "Purinergic agonists stimulate lens Na-K-ATPase-mediated transport via a Src tyrosine kinase-dependent pathway." American Journal of Physiology-Cell Physiology 293, no. 2 (2007): C790—C796. http://dx.doi.org/10.1152/ajpcell.00579.2006.

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The Na-K-ATPase is vital for maintenance of lens transparency. Past studies using intact lens suggested the involvement of tyrosine kinases in short-term regulation of Na-K-ATPase. Furthermore, in vitro phosphorylation of a lens epithelial membrane preparation by Src family kinases (SFKs), a family of nonreceptor tyrosine kinases, resulted in modification of Na-K-ATPase activity. Here, the effect of purinergic agonists, ATP and UTP, on Na-K-ATPase function and SFK activation was examined in the rabbit lens. Na-K-ATPase function was examined using two different approaches, measurement of ouabai

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18

Priyadarshana, Chathura, Rangga Setiawan, Atsushi Tajima, and Atsushi Asano. "Src family kinases-mediated negative regulation of sperm acrosome reaction in chickens (Gallus gallus domesticus)." PLOS ONE 15, no. 11 (2020): e0241181. http://dx.doi.org/10.1371/journal.pone.0241181.

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The acrosome reaction (AR) is a strictly-regulated, synchronous exocytosis that is required for sperm to penetrate ova. This all-or-nothing process occurs only once in the sperm lifecycle through a sequence of signaling pathways. Spontaneous, premature AR therefore compromises fertilization potential. Although protein kinase A (PKA) pathways play a central role in AR across species, the signaling network used for AR induction is poorly understood in birds. Mechanistic studies of mammalian sperm AR demonstrate that PKA activity is downstreamly regulated by Src family kinases (SFKs). Using SFK i

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19

Bagnato, Giulia, Martina Leopizzi, Enrica Urciuoli, and Barbara Peruzzi. "Nuclear Functions of the Tyrosine Kinase Src." International Journal of Molecular Sciences 21, no. 8 (2020): 2675. http://dx.doi.org/10.3390/ijms21082675.

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Src is the representative member of the Src-family kinases (SFKs), a group of tyrosine kinases involved in several cellular processes. Its main function has been for long confined to the plasma membrane/cytoplasm compartment, being a myristoylated protein anchored to the cell membrane and functioning downstream to receptors, most of them lacking intrinsic kinase activity. In the last decades, new roles for some SFKs have been described in the nuclear compartment, suggesting that these proteins can also be involved in directly regulating gene transcription or nucleoskeleton architecture. In thi

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20

Berndt, Sandra, and Ines Liebscher. "New Structural Perspectives in G Protein-Coupled Receptor-Mediated Src Family Kinase Activation." International Journal of Molecular Sciences 22, no. 12 (2021): 6489. http://dx.doi.org/10.3390/ijms22126489.

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Src family kinases (SFKs) are key regulators of cell proliferation, differentiation, and survival. The expression of these non-receptor tyrosine kinases is strongly correlated with cancer development and tumor progression. Thus, this family of proteins serves as an attractive drug target. The activation of SFKs can occur via multiple signaling pathways, yet many of them are poorly understood. Here, we summarize the current knowledge on G protein-coupled receptor (GPCR)-mediated regulation of SFKs, which is of considerable interest because GPCRs are among the most widely used pharmaceutical tar

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Nagy, Zoltan, Jun Mori, Vanesa-Sindi Ivanova, Alexandra Mazharian, and Yotis A. Senis. "Interplay between the tyrosine kinases Chk and Csk and phosphatase PTPRJ is critical for regulating platelets in mice." Blood 135, no. 18 (2020): 1574–87. http://dx.doi.org/10.1182/blood.2019002848.

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Abstract The Src family kinases (SFKs) Src, Lyn, and Fyn are essential for platelet activation and also involved in megakaryocyte (MK) development and platelet production. Platelet SFKs are inhibited by C-terminal Src kinase (Csk), which phosphorylates a conserved tyrosine in their C-terminal tail, and are activated by the receptor-type tyrosine phosphatase PTPRJ (CD148, DEP-1), which dephosphorylates the same residue. Deletion of Csk and PTPRJ in the MK lineage in mice results in increased SFK activity, but paradoxically hypoactive platelets resulting from negative feedback mechanisms, includ

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22

Jin, Wook. "Regulation of Src Family Kinases during Colorectal Cancer Development and Its Clinical Implications." Cancers 12, no. 5 (2020): 1339. http://dx.doi.org/10.3390/cancers12051339.

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Src family kinases (SFKs) are non-receptor kinases that play a critical role in the pathogenesis of colorectal cancer (CRC). The expression and activity of SFKs are upregulated in patients with CRC. Activation of SFKs promotes CRC cell proliferation, metastases to other organs and chemoresistance, as well as the formation of cancer stem cells (CSCs). The enhanced expression level of Src is associated with decreased survival in patients with CRC. Src-mediated regulation of CRC progression involves various membrane receptors, modulators, and suppressors, which regulate Src activation and its dow

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23

Vara, Juan Ángel Fresno, Ma Aurora Domı́nguez Cáceres, Augusto Silva, and Jorge Martı́n-Pérez. "Src Family Kinases Are Required for Prolactin Induction of Cell Proliferation." Molecular Biology of the Cell 12, no. 7 (2001): 2171–83. http://dx.doi.org/10.1091/mbc.12.7.2171.

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Prolactin (PRL) is a pleiotropic cytokine promoting cellular proliferation and differentiation. Because PRL activates the Src family of tyrosine kinases (SFK), we have studied the role of these kinases in PRL cell proliferation signaling. PRL induced [3H]thymidine incorporation upon transient transfection of BaF-3 cells with the PRL receptor. This effect was inhibited by cotransfection with the dominant negative mutant of c-Src (K>A295/Y>F527, SrcDM). The role of SFK in PRL-induced proliferation was confirmed in the BaF-3 PRL receptor-stable transfectant, W53 cells, where PRL induced Fyn

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Tanaka, Masamitsu, Kazuki Sasaki, Reiko Kamata, Yukari Hoshino, Kazuyoshi Yanagihara, and Ryuichi Sakai. "A Novel RNA-Binding Protein, Ossa/C9orf10, Regulates Activity of Src Kinases To Protect Cells from Oxidative Stress-Induced Apoptosis." Molecular and Cellular Biology 29, no. 2 (2008): 402–13. http://dx.doi.org/10.1128/mcb.01035-08.

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ABSTRACT During the process of tumor progression and clinical treatments, tumor cells are exposed to oxidative stress. Tumor cells are frequently resistant to such stress by producing antiapoptotic signaling, including activation of Src family kinases (SFKs), although the molecular mechanism is not clear. In an attempt to identify the SFK-binding proteins selectively phosphorylated in gastric scirrhous carcinoma, we identified an uncharacterized protein, C9orf10. Here we report that C9orf10 (designated Ossa for oxidative stress-associated Src activator) is a novel RNA-binding protein that guar

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Rathore, Vipul B., Masato Okada, Peter J. Newman, and Debra K. Newman. "Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets." Biochemical Journal 403, no. 2 (2007): 275–81. http://dx.doi.org/10.1042/bj20061618.

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SFKs (Src family kinases) contribute importantly to platelet function in haemostasis. SFK activity is controlled by Csk (C-terminal Src kinase), which phosphorylates a C-terminal tyrosine residue on SFKs, resulting in inhibition of SFK activity. Csk is recruited to sites of SFK activity by tyrosine-phosphorylated Csk-binding proteins. Paxillin, a multidomain adaptor protein, has been shown to act as a Csk-binding protein and to inhibit Src activity during growth factor signalling. Human platelets express Hic-5, a member of the paxillin family; however, its ability to act as a Csk-binding prote

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Martellucci, Stefano, Letizia Clementi, Samantha Sabetta, Vincenzo Mattei, Lorenzo Botta, and Adriano Angelucci. "Src Family Kinases as Therapeutic Targets in Advanced Solid Tumors: What We Have Learned So Far." Cancers 12, no. 6 (2020): 1448. http://dx.doi.org/10.3390/cancers12061448.

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Src is the prototypal member of Src Family tyrosine Kinases (SFKs), a large non-receptor kinase class that controls multiple signaling pathways in animal cells. SFKs activation is necessary for the mitogenic signal from many growth factors, but also for the acquisition of migratory and invasive phenotype. Indeed, oncogenic activation of SFKs has been demonstrated to play an important role in solid cancers; promoting tumor growth and formation of distant metastases. Several drugs targeting SFKs have been developed and tested in preclinical models and many of them have successfully reached clini

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Katoh, Kazuo. "Regulation of Fibroblast Cell Polarity by Src Tyrosine Kinase." Biomedicines 9, no. 2 (2021): 135. http://dx.doi.org/10.3390/biomedicines9020135.

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Src protein tyrosine kinases (SFKs) are a family of nonreceptor tyrosine kinases that are localized beneath the plasma membrane and are activated during cell adhesion, migration, and elongation. Due to their involvement in the activation of signal transduction cascades, SFKs have been suggested to play important roles in the determination of cell polarity during cell extension and elongation. However, the mechanism underlying Src-mediated polarity formation remains unclear. The present study was performed to investigate the mechanisms underlying Src-induced cell polarity formation and cell elo

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Ichikawa-Tomikawa, Naoki, Kotaro Sugimoto, Korehito Kashiwagi, and Hideki Chiba. "The Src-Family Kinases SRC and BLK Contribute to the CLDN6-Adhesion Signaling." Cells 12, no. 13 (2023): 1696. http://dx.doi.org/10.3390/cells12131696.

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Cell adhesion molecules, including integrins, cadherins, and claudins (CLDNs), are known to activate Src-family kinases (SFKs) that organize a variety of physiological and pathological processes; however, the underlying molecular basis remains unclear. Here, we identify the SFK members that are coupled with the CLDN6-adhesion signaling. Among SFK subtypes, BLK, FGR, HCK, and SRC were highly expressed in F9 cells and concentrated with CLDN6 along cell borders during epithelial differentiation. Immunoprecipitation assay showed that BLK and SRC, but not FGR or HCK, form a complex with CLDN6 via t

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Sen, Banibrata, and Faye M. Johnson. "Regulation of Src Family Kinases in Human Cancers." Journal of Signal Transduction 2011 (April 4, 2011): 1–14. http://dx.doi.org/10.1155/2011/865819.

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The nonreceptor protein tyrosine kinase Src plays a crucial role in the signal transduction pathways involved in cell division, motility, adhesion, and survival in both normal and cancer cells. Although the Src family kinases (SFKs) are activated in various types of cancers, the exact mechanisms through which they contribute to the progression of individual tumors remain to be defined. The activation of Src in human cancers may occur through a variety of mechanisms that include domain interaction and structural remodeling in response to various activators or upstream kinases and phosphatastes.

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Teixeira, João, Héctor Fuentes, Stasė Bielskutė, et al. "The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain." Molecules 23, no. 11 (2018): 2731. http://dx.doi.org/10.3390/molecules23112731.

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The function of the intrinsically disordered Unique domain of the Src family of tyrosine kinases (SFK), where the largest differences between family members are concentrated, remains poorly understood. Recent studies in c-Src have demonstrated that the Unique region forms transient interactions, described as an intramolecular fuzzy complex, with the SH3 domain and suggested that similar complexes could be formed by other SFKs. Src and Lyn are members of a distinct subfamily of SFKs. Lyn is a key player in the immunologic response and exists in two isoforms originating from alternative splicing

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Colognato, Holly, Shwetha Ramachandrappa, Inger M. Olsen, and Charles ffrench-Constant. "Integrins direct Src family kinases to regulate distinct phases of oligodendrocyte development." Journal of Cell Biology 167, no. 2 (2004): 365–75. http://dx.doi.org/10.1083/jcb.200404076.

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Specific integrins expressed on oligodendrocytes, the myelin-forming cells of the central nervous system, promote either differentiation and survival or proliferation by amplification of growth factor signaling. Here, we report that the Src family kinases (SFKs) Fyn and Lyn regulate each of these distinct integrin-driven behaviors. Fyn associates with α6β1 and is required to amplify platelet-derived growth factor survival signaling, to promote myelin membrane formation, and to switch neuregulin signaling from a phosphatidylinositol 3-kinase to a mitogen-activated protein kinase pathway (thereb

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Knox, Renatta, and Xiangning Jiang. "Fyn in Neurodevelopment and Ischemic Brain Injury." Developmental Neuroscience 37, no. 4-5 (2015): 311–20. http://dx.doi.org/10.1159/000369995.

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The Src family kinases (SFKs) are nonreceptor protein tyrosine kinases that are implicated in many normal and pathological processes in the nervous system. The SFKs Fyn, Src, Yes, Lyn, and Lck are expressed in the brain. This review will focus on Fyn, as Fyn mutant mice have striking phenotypes in the brain and Fyn has been shown to be involved in ischemic brain injury in adult rodents and, with our work, in neonatal animals. An understanding of Fyn's role in neurodevelopment and disease will allow researchers to target pathological pathways while preserving protective ones.

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Piazza, Timothy M., Juu-Chin Lu, Kristopher C. Carver, and Linda A. Schuler. "Src Family Kinases Accelerate Prolactin Receptor Internalization, Modulating Trafficking and Signaling in Breast Cancer Cells." Molecular Endocrinology 23, no. 2 (2009): 202–12. http://dx.doi.org/10.1210/me.2008-0341.

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Abstract Despite the growing body of evidence supporting prolactin (PRL) actions in human breast cancer, little is known regarding PRL regulation of its own receptor in these cells. Ligand-initiated endocytosis is a key process in the regulation of receptor availability and signaling cascades that may lead to oncogenic actions. Although exposure to exogenous PRL accelerates degradation of the long isoform of the PRL receptor (lPRLR), neither the signals initiated by PRL that lead to lPRLR internalization and subsequent down-regulation, nor the relationship to downstream pathways are understood

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Lannutti, Brian J., and Jonathan G. Drachman. "Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of hematopoietic cell lines and primary megakaryocytic progenitors." Blood 103, no. 10 (2004): 3736–43. http://dx.doi.org/10.1182/blood-2003-10-3566.

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Abstract In this study we demonstrate that thrombopoietin (TPO)–stimulated Src family kinases (SFKs) inhibit cellular proliferation and megakaryocyte differentiation. Using the Src kinase inhibitors pyrolopyrimidine 1 and 2 (PP1, PP2), we show that TPO-dependent proliferation of BaF3/Mpl cells was enhanced at concentrations that are specific for SFKs. Similarly, proliferation is increased after introducing a dominant-negative form of Lyn into BaF3/Mpl cells. Murine marrow cells from Lyn-deficient mice or wild-type mice cultured in the presence of the Src inhibitor, PP1, yielded a greater numbe

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Cary, Leslie A., Richard A. Klinghoffer, Christoph Sachsenmaier, and Jonathan A. Cooper. "Src Catalytic but Not Scaffolding Function Is Needed for Integrin-Regulated Tyrosine Phosphorylation, Cell Migration, and Cell Spreading." Molecular and Cellular Biology 22, no. 8 (2002): 2427–40. http://dx.doi.org/10.1128/mcb.22.8.2427-2440.2002.

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ABSTRACT Src family kinases (SFKs) are crucial for signaling through a variety of cell surface receptors, including integrins. There is evidence that integrin activation induces focal adhesion kinase (FAK) autophosphorylation at Y397 and that Src binds to and is activated by FAK to carry out subsequent phosphorylation events. However, it has also been suggested that Src functions as a scaffolding molecule through its SH2 and SH3 domains and that its kinase activity is not necessary. To examine the role of SFKs in integrin signaling, we have expressed various Src molecules in fibroblasts lackin

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36

Wayne, Chad M., Heng-Yu Fan, Xiaodong Cheng, and JoAnne S. Richards. "Follicle-Stimulating Hormone Induces Multiple Signaling Cascades: Evidence that Activation of Rous Sarcoma Oncogene, RAS, and the Epidermal Growth Factor Receptor Are Critical for Granulosa Cell Differentiation." Molecular Endocrinology 21, no. 8 (2007): 1940–57. http://dx.doi.org/10.1210/me.2007-0020.

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Abstract FSH regulates ovarian granulosa cell differentiation not only by activating adenylyl cyclase and protein kinase A (PKA) but also by other complex mechanisms. Using primary rat granulosa cell cultures, we provide novel evidence that FSH rapidly activates two small GTP-binding proteins RAP1 and RAS. FSH activation of RAP1 requires cAMP-mediated activation of exchange factor activated by cAMP/RAPGEF3 whereas FSH activation of RAS and downstream signaling cascades involves multiple factors. Specifically, FSH activation of RAS required Rous sarcoma oncogene (SRC) family tyrosine kinase (SF

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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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Mittaud, Peggy, Alain A. Camilleri, Raffaella Willmann, Susanne Erb-Vögtli, Steven J. Burden, and Christian Fuhrer. "A Single Pulse of Agrin Triggers a Pathway That Acts To Cluster Acetylcholine Receptors." Molecular and Cellular Biology 24, no. 18 (2004): 7841–54. http://dx.doi.org/10.1128/mcb.24.18.7841-7854.2004.

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ABSTRACT Agrin triggers signaling mechanisms of high temporal and spatial specificity to achieve phosphorylation, clustering, and stabilization of postsynaptic acetylcholine receptors (AChRs). Agrin transiently activates the kinase MuSK; MuSK activation has largely vanished when AChR clusters appear. Thus, a tyrosine kinase cascade acts downstream from MuSK, as illustrated by the agrin-evoked long-lasting activation of Src family kinases (SFKs) and their requirement for AChR cluster stabilization. We have investigated this cascade and report that pharmacological inhibition of SFKs reduces earl

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Bauer, S., G. D. Demetri, and J. A. Fletcher. "Evaluation of SRC-family kinases in gastrointestinal stromal tumors." Journal of Clinical Oncology 24, no. 18_suppl (2006): 9529. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.9529.

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9529 Background: Inhibition of KIT oncoproteins by imatinib mesylate (IM) induces clinical responses in most GIST patients. However, many patients develop IM-resistance and novel KIT-Inhibitors show clinical benefit in only a minority of patients. SRC-family kinases (SFK) are important participants in kinase oncoprotein signaling pathways in ALL and CML, and dual-specificity SRC/ABL-inhibitors show promising activity in IM-resistant CML in vitro. However, little is known about SFK functional roles in IM-resistant GIST. Methods: GIST were analyzed for SFK expression and activation by western bl

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Zereg, Elamine, Laure Voisin, Karl Grenier, et al. "Abstract 1675: Investigating the role of SRC-family kinases in MPNST tumorigenesis." Cancer Research 84, no. 6_Supplement (2024): 1675. http://dx.doi.org/10.1158/1538-7445.am2024-1675.

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Abstract Purpose: Malignant peripheral nerve sheath tumor (MPNST), an aggressive soft-tissue sarcoma, is the leading cause of mortality in patients with neurofibromatosis type 1. Over the past two decades, significant advancement has been made in understanding the pathogenesis of MPNST. Still, this progress has not improved overall survival of patients. Therefore, ongoing efforts to identify alterations contributing to the transformation, progression, and metastasis of MPNST are essential for pinpointing targetable oncogenic signaling pathways for this cancer. Previous studies have revealed an

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Imada, Shinya, Yoji Murata, Takenori Kotani, et al. "Role of Src Family Kinases in Regulation of Intestinal Epithelial Homeostasis." Molecular and Cellular Biology 36, no. 22 (2016): 2811–23. http://dx.doi.org/10.1128/mcb.00311-16.

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Proper regulation of epithelial cell turnover is important for the structural integrity and homeostasis of various tissues, including the intestine. Here we show that ablation of Csk, a negative regulator of Src family kinases (SFKs), specifically in intestinal epithelial cells (IECs) resulted in the development of hyperplasia throughout the intestinal epithelium of mice. Such conditional ablation of Csk also increased the proliferative activity and turnover of IECs, disturbed the differentiation of Paneth and goblet cells, reduced the number of intestinal stem cells, and attenuated the expres

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Xiao, Xiang, Ya Ni, Chenhuan Yu, et al. "Src family kinases (SFKs) and cell polarity in the testis." Seminars in Cell & Developmental Biology 81 (September 2018): 46–53. http://dx.doi.org/10.1016/j.semcdb.2017.11.024.

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Harrison, M., G. Nash, S. Watson, and G. Rainger. "Platelet SRC family kinases (SFKS) mediate leukocyte recruitment in atherosclerosis." Atherosclerosis 241, no. 1 (2015): e42. http://dx.doi.org/10.1016/j.atherosclerosis.2015.04.151.

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Nie, Lingdi, Liwen Jiang, John Quinn, Blair Grubb, and Minyan Wang. "TRPA1-Mediated Src Family Kinases Activity Facilitates Cortical Spreading Depression Susceptibility and Trigeminovascular System Sensitization." International Journal of Molecular Sciences 22, no. 22 (2021): 12273. http://dx.doi.org/10.3390/ijms222212273.

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Transient receptor potential ankyrin 1 (TRPA1) plays a role in migraine and is proposed as a promising target for migraine therapy. However, TRPA1-induced signaling in migraine pathogenesis is poorly understood. In this study, we explored the hypothesis that Src family kinases (SFKs) transmit TRPA1 signaling in regulating cortical spreading depression (CSD), calcitonin gene-related peptide (CGRP) release and neuroinflammation. CSD was monitored in mouse brain slices via intrinsic optical imaging, and in rats using electrophysiology. CGRP level and IL-1β gene expression in mouse trigeminal gang

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Dos Santos, Cedric, Tinisha McDonald, Yin Wei Ho, et al. "The Src and c-Kit kinase inhibitor dasatinib enhances p53-mediated targeting of human acute myeloid leukemia stem cells by chemotherapeutic agents." Blood 122, no. 11 (2013): 1900–1913. http://dx.doi.org/10.1182/blood-2012-11-466425.

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Key Points SRC family kinases are activated in AML stem/progenitor cells and contribute to AML stem cell survival and proliferation. Combined inhibition of SFKs and c-KIT with dasatinib enhances p53-mediated elimination of AML stem cells.

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Ren, Liangliang, Chaoying Li, Youliang Wang, et al. "In Vivo Phosphoproteome Analysis Reveals Kinome Reprogramming in Hepatocellular Carcinoma." Molecular & Cellular Proteomics 17, no. 6 (2018): 1067–83. http://dx.doi.org/10.1074/mcp.ra117.000421.

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Aberrant kinases contribute to cancer survival and proliferation. Here, we quantitatively characterized phosphoproteomic changes in an HBx-transgenic mouse model of hepatocellular carcinoma (HCC) using high-resolution mass spectrometry, profiled 22,539 phosphorylation sites on 5431 proteins. Using a strategy to interpret kinase- substrate relations in HCC and to uncover predominant kinases in tumors, our results, revealed elevated kinase activities of Src family kinases (SFKs), PKCs, MAPKs, and ROCK2 in HCC, representatives of which were further validated in cell models and clinical HBV-positi

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Zhao, Xiaoxian, Andrew E. Schade, and Eric Hsi. "Distinct Role of Src Family Kinase Inhibitors in Burkitt Lymphoma Cells Vs. Diffuse Large B-Cell Lymphoma Cells." Blood 112, no. 11 (2008): 3765. http://dx.doi.org/10.1182/blood.v112.11.3765.3765.

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Abstract Introduction: The Non-Hodgkin lymphomas (NHLs) are a heterogeneous group of malignancies, with approximately 85% of NHL belonging to the B-cell lineage. Src family kinases (SFKs) are non-receptor intracellular tyrosine kinases which are important in the regulation of multiple signaling pathways including cell proliferation, tumor invasiveness, angiogenesis and apoptosis. Syk is another predominant tyrosine kinase expressed in B-cell lines in addition to SFKs. We attempted to correlate SFK and Syk inhibitor efficacy with the presence of phospho-SFK or phospho-Syk in lymphoma cell lines

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Huang, Hui, Zachary Waldon, Gordon Chan, et al. "Tyrosine Phosphorylation of Runx1 In Megakaryocytes by Src Family Kinases." Blood 116, no. 21 (2010): 742. http://dx.doi.org/10.1182/blood.v116.21.742.742.

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Abstract Abstract 742 Runx1 and its cofactor, CBF-beta, are the most frequent targets of chromosomal translocations in human leukemias. Point mutations in Runx-1 also occur in some cases of myelodysplastic syndrome and undifferentiated leukemia. During normal hematopoiesis, Runx1 is required for the ontogeny of all definitive hematopoietic stem cells and for the proper maturation of megakaryocytes (Mks) and lymphocytes. Despite these critical roles, the regulation of Runx1 activity via cell signaling pathways remains incompletely understood. Here, we report that Runx-1 is tyrosine phosphorylat

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Piemonte, Katrina, Elyse Donaubauer, and Ruth Keri. "Abstract PD3-06: The SRC family kinase, YES1, controls chromosomal stability and promotes growth of triple negative breast cancer." Cancer Research 82, no. 4_Supplement (2022): PD3–06—PD3–06. http://dx.doi.org/10.1158/1538-7445.sabcs21-pd3-06.

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Abstract Triple negative breast cancer (TNBC) is a collection of heterogeneous diseases with limited therapeutic options primarily involving cytotoxic chemotherapy. The distinct molecular profile and increased chromosomal instability (CIN) of TNBC make it a difficult disease to treat. While many patients initially respond to treatment, resistance is common, resulting in poor patient outcomes. Thus identifying vulnerabilities in this disease is necessary to improve TNBC patient outcomes. To identify potential therapeutic targets in this disease, we focused on Src Family Kinases (SFKs). The SFK

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Kook, Eunjin, Kyung-Soo Chun, and Do-Hee Kim. "Emerging Roles of YES1 in Cancer: The Putative Target in Drug Resistance." International Journal of Molecular Sciences 25, no. 3 (2024): 1450. http://dx.doi.org/10.3390/ijms25031450.

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Src family kinases (SFKs) are non-receptor tyrosine kinases that are recognized as proto-oncogenic products. Among SFKs, YES1 is frequently amplified and overexpressed in a variety of human tumors, including lung, breast, ovarian, and skin cancers. YES1 plays a pivotal role in promoting cell proliferation, survival, and invasiveness during tumor development. Recent findings indicate that YES1 expression and activation are associated with resistance to chemotherapeutic drugs and tyrosine kinase inhibitors in human malignancies. YES1 undergoes post-translational modifications, such as lipidation

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