| Abstract [eng] |
Extracellular and intracellular signals are mediated by protein-protein interactions. These interactions are determined by specialized protein domains, for example, Src homology (SH) domains found in many proteins. Nck family proteins, Nck-α and Nck-β, are composed of three SH3 and one SH2 domains and have no any putative catalytic domain. Nck proteins act as adaptors by linking via SH2 and SH3 domains proteins that regulate various intracellular processes. Here we show that Nck family proteins associate with RasGAP constantly in vivo and in vitro, but after PDGFR-β stimulation quantity of Nck-bound RasGAP increases. Constant interaction depends on Nck-α SH2 and one or several SH3 domains. SH2 domain is responsible for binding of additional RasGAP after PDGFR-β stimulation. We have also determined that Nck proteins are able to interact with RasGAP directly. One or several SH3 domains are responsible for Nck-a direct association with RasGAP. Immunofluorescence assay show that localization patterns of Nck-a and RasGAP are similar. |
