Nck proteins are a family of SH2/SH3 domain-containing adaptor proteins. Both Nck-α and Nck-β play a major role in regulating a wide variety of cellular processes, including cytoskeletal rearrangement, cell morphology, gene expression and protein translation. We have analysed proteins interacting with SH3 domains of Nck-α. The proteins were separated using two-dimensional electrophoresis, subjected to in-gel digestion with trypsin and identified by mass spectrometry using MALDI-TOF mass fingerprinting. Here we report novel potential binding partners for Nck-α such as 14-3-3γ protein, eukaryotic translation initiation factor 4E and ras-related protein Rab-30. Our results provide additional information presumably confirming Nck-α role in actin cytoskeleton rearrangement regulation and the modulation of the eukaryotic translation initiation. Data also suggest that Nck-α might be involved in the control of Golgi functioning.

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