The Src homology (SH) domains are protein modules found in many different proteins. The Nck family proteins consist of Nck-α and Nck-β proteins composed entirely of SH2 and SH3 domains and have no any putative catal ytic domain. These proteins act as adaptors by linking tyrosine-phosphorylated proteins to other signaling molecules. Here we show that Nck-β associates with the ligand-stimulated platelet-derived growth factor (PDGF) receptor-β and Ras GTPase-activating protein (RasGAP) in vivo. Nck-β interaction with RasGAP is constant, but also increases after PDGF receptor-β stimulation. In contrast, Nck-α does not interact with ligand-activated PDGF receptor-β, but constantly associates with RasGAP.

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