Src Kinases

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Src Kinases Background

About Src Kinases

The Src family of kinases (SFK) is a non-receptor tyrosine kinase named after the first recognized member, v-Src, which was isolated from Rauschert's sarcoma virus. Src kinases are highly conserved across species and are involved in the regulation of a wide range of cellular processes, including the regulation of important cellular functions such as cell proliferation, differentiation, apoptosis, migration, and metabolism. The vertebrate Src kinase family consists of nine members, namely SRC, LCK, LYN, BLK, HCK, FYN, FGR, YES, and YRK. Note that YRK is expressed only in chickens.

Src family kinases contain six distinct domains including a myristoylated N-terminal segment, an SH2 domain, an SH3 domain, a linker region, a tyrosine kinase domain, and a C-terminal segment. Src kinases are known for having a characteristically short C-terminal tail that contains an autoinhibitory phosphorylation site. The SH2 and SH3 domains exist in a conformation that locks the catalytic domain into an inactive state.

Src family kinases interact with many cellular cytosolic, nuclear, and membrane proteins, modifying these proteins by phosphorylation of tyrosine residues. Some substrates have been discovered for these enzymes. Dysregulation (including constitutive activation or overexpression) may lead to the degradation of cellular function and may also lead to the progression of cellular transformation and oncogenic activity.

Src family kinases (SFKs). Fig.1 Src family kinases (SFKs). (Ohnishi H, et al., 2011)

Mechanism of Action of Src Kinases

The activation of Src kinases is tightly regulated and involves several steps. In their inactive state, Src kinases adopt a closed conformation, where an inhibitory phosphorylation at a tyrosine residue near the C-terminus maintains their inactivity. Upon activation of upstream signaling pathways, such as receptor tyrosine kinases or G-protein-coupled receptors, this inhibitory phosphorylation is removed by phosphatases, resulting in the activation of Src kinases. Once activated, Src kinases can phosphorylate various downstream targets, including other kinases, adaptor proteins, and cytoskeletal proteins, thereby initiating signaling cascades.

Functions of Src Kinases

Src kinases have diverse functions in different cellular processes. Here are some examples of their functions:

  • Cell Growth and Proliferation

Src kinases are involved in the regulation of cell growth and proliferation through their influence on multiple signaling pathways, including the Ras-MAPK pathway and the PI3K-Akt pathway. They can modulate the activity of growth factor receptors and downstream effectors involved in cell cycle progression.

  • Cell Migration and Adhesion

Src kinases play a critical role in cell migration and adhesion by regulating the dynamics of the cytoskeleton and focal adhesion complexes. They can phosphorylate proteins involved in actin remodeling, such as focal adhesion kinase (FAK), leading to the formation of focal adhesions and the promotion of cell migration.

  • Signal Transduction

Src kinases participate in the transmission of signals from various cell surface receptors, including receptor tyrosine kinases and G-protein-coupled receptors. They can phosphorylate downstream signaling molecules, such as STAT proteins, MAP kinases, and transcription factors, thereby regulating gene expression and cellular responses.

  • Cancer, Inflammation, and Immune Disorders

Dysregulation of Src kinases has been implicated in inflammation, immune disorders, cancer development and progression. Aberrant activation of Src kinases can lead to uncontrolled cell growth, increased cell motility, and enhanced invasive properties, promoting tumor formation and metastasis. Therefore, Src kinases have emerged as potential targets for cancer therapy.

Src and other Src family protein tyrosine kinases are proto-oncogenes that play key roles in regulating cell growth and differentiation. Src family activity is regulated by tyrosine phosphorylation at two sites with opposing effects. Phosphorylation at Y419 of human Src up-regulates kinase activity, while phosphorylation at Y530 inactivates Src.

Src signaling in cancer invasion.Fig.2 Src signaling in cancer invasion. (Abbaspour Babaei M, et al., 2016)

Available Resources for Src Kinases

Understanding the role of Src kinases in cell signaling is critical to unraveling the complexity of various biological processes and developing targeted therapies. At Creative BioMart, we offer a wide range of research tools and services to support Src kinase-related studies, including assay kits, recombinant proteins, cell & tissue lysates, protein pre-coupled magnetic beads, and custom assay development. The following Src kinases are displayed, click to view all related molecules/targets and research reagents. Please feel free to contact us with any questions or requests.


  1. Ohnishi H, Murata Y, Okazawa H, Matozaki T. Src family kinases: modulators of neurotransmitter receptor function and behavior. Trends Neurosci. 2011;34(12):629-637.
  2. Parsons S J, Parsons J T. Src family kinases, key regulators of signal transduction[J]. Oncogene, 2004, 23(48): 7906-7909.
  3. Abbaspour Babaei M, Kamalidehghan B, Saleem M, et al. Receptor tyrosine kinase (c-Kit) inhibitors: a potential therapeutic target in cancer cells[J]. Drug design, development, and therapy, 2016: 2443-2459.


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