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Background: Focal adhesion kinase 2 (FAK2), which is highly expressed in the central nervous system, is rapidly phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by protein kinase C activation. Activation of FAK2 leads to modulation of ion channel function and activation of the MAP kinase signalling pathway. FAK2 activation may provide a mechanism for a variety of short- and long-term calcium-dependent signalling events in the nervous system (1). FAK2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. Pap has been identified as a new Pyk2 binding protein. It has been demonstrated that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap (2).