Reactome | PTK2 autophosphorylates

PTK2 autophosphorylates

Stable Identifier

R-HSA-5218642

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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Six tyrosine phosphorylation sites in focal adhesion kinase 1 (FAK1) serve to modulate FAK1 kinase activity or mediate FAK1 interaction with SH2-domain containing proteins. These are Y397, Y407, Y576, Y577, Y861 and Y925 (Mitra et al. 2005). They are differentially phosphorylated by diverse agonists and implicated in transmitting different signals and effects (Ciccimaro et al. 2006, Le Boeuf et al. 2004,2006). Y397 is the major autophosphorylation site present upstream of the FAK kinase domain (Schaller et al. 1994). In response to VEGF stimulation FAK1 is recruited and autophosphorylated at Y397. This phosphorylated tyrosine then creates a binding site for other signaling proteins that link FAK1 to downstream signaling pathways and the actin cytoskeleton (Toutant et al. 2002).

Literature References

PubMed ID	Title	Journal	Year
15688067	Focal adhesion kinase: in command and control of cell motility Mitra, SK, Schlaepfer, DD, Hanson, DA	Nat Rev Mol Cell Biol	2005
12391143	Alternative splicing controls the mechanisms of FAK autophosphorylation Studler, JM, Carnaud, M, Costa, A, Toutant, M, Kadaré, G, Girault, JA	Mol. Cell. Biol.	2002