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

• Published in: The Journal of biological chemistry 1994-06, Vol.269 (23), p.16009-16014
• Main Authors: SEEDORF, K, KOSTKA, G, LAMMERS, R, BASHKIN, P, DALY, R, BURGESS, W. H, VAN DER BLIEK, A. M, SCHLESSINGER, J, ULLRICH, A
• Format: Article
• Language: English
• Subjects: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Biological and medical sciences; Cell physiology; Cell structures and functions; Cytoskeleton, cytoplasm. Intracellular movements; Dynamins; Fundamental and applied biological sciences. Psychology; Genes, src; Glutathione Transferase - genetics; GRB2 Adaptor Protein; GTP Phosphohydrolases - metabolism; Humans; Microtubules - enzymology; Molecular and cellular biology; Molecular Sequence Data; Protein Binding; Protein Conformation; Proteins - metabolism; Recombinant Fusion Proteins; Signal Transduction; Type C Phospholipases - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(17)33965-0

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.