Src: Difference between revisions

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{{Infobox protein
| name = Src
| image = Src_structure.png
| caption = Crystal structure of Src kinase
| symbol = SRC
| HGNCid = 11283
| OMIM = 190090
| EntrezGene = 6714
| RefSeq = NM_005417
| UniProt = P12931
}}
'''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.

Also see[edit]

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