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

• Published in: The Journal of biological chemistry Vol. 269; no. 23; pp. 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: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 10.06.1994
• 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; Signal transduction; Enzyme; Proline; Cytoskeleton; Hydrolases; Molecular interaction; Esterases; Microtubule associated protein; Binding site; Phosphoric diester hydrolases; Phospholipase C

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 pro...