Src: Difference between revisions
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'''Src''' is a non-receptor [[tyrosine kinase]] that plays a critical role in the regulation of cellular processes, including proliferation, differentiation, and survival. It is a member of the Src family kinases (SFKs), which are involved in the signaling pathways of various cellular receptors. | '''Src''' is a non-receptor [[tyrosine kinase]] that plays a critical role in the regulation of cellular processes, including proliferation, differentiation, and survival. It is a member of the Src family kinases (SFKs), which are involved in the signaling pathways of various cellular receptors. | ||
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* [[Oncogene]] | * [[Oncogene]] | ||
* [[Protein phosphorylation]] | * [[Protein phosphorylation]] | ||
{{Protein-stub}} | {{Protein-stub}} | ||
[[Category:Tyrosine kinases]] | [[Category:Tyrosine kinases]] | ||
[[Category:Oncogenes]] | [[Category:Oncogenes]] | ||
[[Category:Signal transduction]] | [[Category:Signal transduction]] | ||
Latest revision as of 23:22, 30 December 2024
Src is a non-receptor tyrosine kinase that plays a critical role in the regulation of cellular processes, including proliferation, differentiation, and survival. It is a member of the Src family kinases (SFKs), which are involved in the signaling pathways of various cellular receptors.
Structure[edit]
Src is composed of several domains that contribute to its function:
- SH3 domain: This domain binds to proline-rich sequences and is involved in protein-protein interactions.
- SH2 domain: This domain binds to phosphorylated tyrosine residues, allowing Src to interact with other phosphorylated proteins.
- Kinase domain: The catalytic domain responsible for the transfer of a phosphate group from ATP to a tyrosine residue on a substrate protein.
- Regulatory tail: The C-terminal tail contains a tyrosine residue that, when phosphorylated, inhibits Src activity.
Function[edit]
Src is involved in the regulation of several cellular processes:
- Cell growth and division: Src promotes cell cycle progression by phosphorylating key proteins involved in the cell cycle.
- Cell adhesion and migration: Src modulates the dynamics of the cytoskeleton and cell adhesion molecules, influencing cell movement.
- Signal transduction: Src is activated by various cell surface receptors, including growth factor receptors, integrins, and G-protein coupled receptors.
Regulation[edit]
Src activity is tightly regulated by phosphorylation:
- Activation: Dephosphorylation of the C-terminal tyrosine residue (Tyr527) leads to Src activation.
- Inhibition: Phosphorylation of Tyr527 by C-terminal Src kinase (Csk) inhibits Src activity.
Clinical Significance[edit]
Src has been implicated in several diseases, particularly cancer:
- Oncogenesis: Overexpression or constitutive activation of Src is associated with the development of various cancers, including breast cancer, colon cancer, and lung cancer.
- Therapeutic target: Src inhibitors, such as dasatinib, are used in the treatment of certain cancers.
Research[edit]
Ongoing research is focused on understanding the precise mechanisms by which Src contributes to cancer progression and identifying novel therapeutic strategies to target Src in cancer.
