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Dynamin binds to SH3 domains of phospholipase C gamma and GRB-2.

Src homology 3 (SH3) domains are found in a variety of proteins that are involved in signal transduction or represent components of the cytoskeleton. These domains are thought to serve as modules that mediate specific protein-protein interactions that include proline-rich sequences on the target protein. We have identified proteins of 110, 80, 65, and 43 kDa in human embryonic fibroblasts that bind specifically to the SH3 domain of phospholipase C gamma, a primary substrate of receptor tyrosine kinases, and characterized the 110-kDa band as the microtubule- activated GTPase dynamin. In addition, dynamin binds the son of sevenless adaptor protein GRB-2 with even higher affinity. This interaction does not require the dynamin GTPase function and involves a proline-rich target sequence between residues 812 and 820 of dynamin.[1]

References

  1. Dynamin binds to SH3 domains of phospholipase C gamma and GRB-2. Seedorf, K., Kostka, G., Lammers, R., Bashkin, P., Daly, R., Burgess, W.H., van der Bliek, A.M., Schlessinger, J., Ullrich, A. J. Biol. Chem. (1994) [Pubmed]
 
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