Drug Target and Biomarker: c-Src (Src) in various biological processes

NCBI ID: G6714

Content of Review Report on SRC Target / Biomarker

SRC

Drug Target and Biomarker: c-Src (Src) in various biological processes

In bone metastasis, c-Src is involved in the activation of FAK and recruitment of other signaling molecules, promoting proliferation and survival of tumor cells.
C-Src plays a role in the regulation of nuclear receptor activity through CLDN-adhesion signaling.
Activation of Src kinase by viruses leads to increased expression of hormone receptors and affects the structure of cervical stroma.
Targeting the ERalpha/Src dimer using specific peptides can restore tamoxifen sensitivity in resistant breast cancer cells.
The presence and activity of Src protein are associated with the development of metastatic phenotypes, and its levels can be used as a prognostic marker.

These viewpoints collectively highlight the diverse roles of c-Src in cancer progression, hormone signaling, and metastasis, emphasizing its significance as a potential therapeutic target in certain contexts.
Based on the provided context information, here are the key viewpoints related to SRC:

Dasatinib, a drug, inhibits the Src-mediated STAT phosphorylation pathway, while the JAK-activation pathway compensates by allowing STAT5 phosphorylation.
Src kinase plays an essential positive regulatory role in amino acid-induced mTORC1 signaling.
Goniothalamin (GTN) induces necroptosis in cancer cells by increasing ROS production, leading to DNA damage and cell membrane rupture. It also induces anoikis, a form of apoptosis-like cell death, in detached cancer cells through the inhibition of survival signaling pathways involving EGFR/FAK/Src.
Src is involved in regulating alpha1 Na/K-ATPase in normal and cancer cells, potentially through various signaling pathways.
In tamoxifen-resistant breast cancer cells, hyperactivated Src leads to the degradation of VHL protein, resulting in the stabilization of KLF4 and endocrine resistance. Blockade of Src activity by Dasatinib prevents VHL degradation and restores the endocrine response.

These findings suggest that Src plays significant roles in various cellular processes, including cytokine signaling, mTORC1 activation, cell death pathways, and endocrine resistance in cancer cells. Src inhibitors like Dasatinib hold potential for targeting Src-mediated pathways in therapeutic interventions for cancer treatment.

Protein Name: SRC Proto-oncogene, Non-receptor Tyrosine Kinase

Functions: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159)

The "SRC Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about SRC comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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