Ptk2 autophosphorylates at Y397

Stable Identifier
Reaction [transition]
Mus musculus
SVG |   | PPTX  | SBGN
Ptk2 autophosphorylates at Y397

Focal adhesion kinase 1 (PTK2, FAK, FAK1) activation plays a critical role in EPHB receptor signaling in dendritic spines. PTK2 has six tyrosine phosphorylation sites, with tyrosine 397 being the main auto-phosphorylation site present upstream of the kinase domain (Schaller et al. 1994). Activation of EPHB receptors induces long-lasting phosphorylation of PTK2 on tyrosine 397 (Shi et al. 2009). This phosphorylated tyrosine then creates a binding site for other signaling proteins that link PTK2 to downstream signaling pathways and actin cytoskeleton.

Literature References
PubMed ID Title Journal Year
7509446 Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

Schaller, MD, Hildebrand, JD, Shannon, JD, Fox, JW, Vines, RR, Parsons, JT

Mol Cell Biol 1994
16298995 EphB receptors regulate dendritic spine morphogenesis through the recruitment/phosphorylation of focal adhesion kinase and RhoA activation

Moeller, ML, Shi, Y, Reichardt, LF, Ethell, IM

J. Biol. Chem. 2006
19553453 Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity

Shi, Y, Pontrello, CG, DeFea, KA, Reichardt, LF, Ethell, IM

J. Neurosci. 2009
Catalyst Activity

protein tyrosine kinase activity of ephrin-B2:Ephb2:FAK1 [plasma membrane]

Orthologous Events
Cite Us!