Reactome | Phosphorylation of PTK2 (FAK) on tyrosine-397 in response to turbulent blood flow

Phosphorylation of PTK2 (FAK) on tyrosine-397 in response to turbulent blood flow

Stable Identifier

R-HSA-9861484

Type

Reaction [uncertain]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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Phosphorylation of PTK2 (FAK) on tyrosine-397 in response to turbulent blood flow

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Binding of integrin alpha5:beta1 to extracellular fibronectin matrix causes the phosphorylation of PTK2 (FAK) on tyrosine-397 through an uncharacterized mechanism (Albarrán-Juárez et al. 2018, also inferred from mouse and bovine endothelial cells in Petzold et al. 2009). Annexin A2, presumably in a complex with integrin alpha5:beta1, is also required for phosphorylation of PTK2 (Zhang et al. 2020).
Within focal adhesions, PTK2 is capable of interacting with phosphoinositol-4.5-bisphosphate, paxillin, talin, beta integrins, and SRC (reviewed in Le Coq et al. 2022). PTK2 can transautophosphorylate serine-397 (Schaller et al. 1994, and inferred from the chicken homolog in Acebrón et al. 2020) and phosphoserine-397 recruits the kinase SRC (Schaller et al. 1994).
During acute initial exposure to laminar shear stress, integrin alphaV:integrin beta3 (ITGAV:ITGB3) enhances phosphorylation of PTK2, but integrin alpha5:integrin beta1 (ITGA5:ITGB1) has no effect.

Literature References

PubMed ID	Title	Journal	Year
32673515	Coupling of Integrin α5 to Annexin A2 by Flow Drives Endothelial Activation Zhang, C, Zhou, T, Chen, Z, Yan, M, Li, B, Lv, H, Wang, C, Xiang, S, Shi, L, Zhu, Y, Ai, D	Circ Res	2020
30194266	Piezo1 and G_q/G₁₁ promote endothelial inflammation depending on flow pattern and integrin activation Albarrán-Juárez, J, Iring, A, Wang, S, Joseph, S, Grimm, M, Strilic, B, Wettschureck, N, Althoff, TF, Offermanns, S	J Exp Med	2018