Organic Photosensitizer Small Molecules in Light-Induced Organic Synthesis: Progress, Mechanisms, and Applications

Jinfeng Shang

doi:10.1002/chem.71200

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3

2026-06-26

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Esa T. Mikkola *

C

Carl G. Gahmberg

DOI：10.1002/1873-3468.70401

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Abstract

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C-terminal Src kinase (Csk) is crucial for the normal function of platelet integrin αIIbβ3 because it inactivates Src kinase. While the molecular mechanism by which cytoplasmic Csk associates with membrane-bound Src is known in resting platelets, it remains unknown in activated platelets. Using surface plasmon resonance, a kinase assay, and microscale thermophoresis, we discovered that Csk binds directly to phospho-Tyr747 on the β3 tail via its SH2 domain and that this binding fully activates Csk. Moreover, we found that phospho-Thr753 on the β3 tail prevents Csk from binding. Collectively, our findings provide new insight into the regulation of Csk function in activated platelets, suggesting that Tyr747-phosphorylated β3 recruits Csk near active Src, whereas phospho-Thr753 on β3 inhibits this interaction.

Keywords:

Csk

integrin beta-3

phosphothreonine

phosphotyrosine

platelet

Src

Src homology 2 domain (SH2 domain)

Src homology 3 domain (SH3 domain)

tyrosine-protein kinase (tyrosine kinase)

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3

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