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  • *src Homology Domains  (1)
  • Animals  (1)
  • Abscisic acid
  • 1995-1999  (1)
  • 1997  (1)
  • 1
    Publication Date: 1997-04-11
    Description: The proline-rich COOH-terminal region of dynamin binds various Src homology 3 (SH3) domain-containing proteins, but the physiological role of these interactions is unknown. In living nerve terminals, the function of the interaction with SH3 domains was examined. Amphiphysin contains an SH3 domain and is a major dynamin binding partner at the synapse. Microinjection of amphiphysin's SH3 domain or of a dynamin peptide containing the SH3 binding site inhibited synaptic vesicle endocytosis at the stage of invaginated clathrin-coated pits, which resulted in an activity-dependent distortion of the synaptic architecture and a depression of transmitter release. These findings demonstrate that SH3-mediated interactions are required for dynamin function and support an essential role of clathrin-mediated endocytosis in synaptic vesicle recycling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shupliakov, O -- Low, P -- Grabs, D -- Gad, H -- Chen, H -- David, C -- Takei, K -- De Camilli, P -- Brodin, L -- CA46128/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):259-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Nobel Institute for Neurophysiology, Department of Neuroscience, Karolinska Institutet, S-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Coated Pits, Cell-Membrane/ultrastructure ; Dynamins ; *Endocytosis ; GTP Phosphohydrolases/*metabolism ; Humans ; Lampreys ; Microscopy, Electron ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*metabolism ; Proline/chemistry ; Recombinant Fusion Proteins/metabolism ; Synapses/metabolism/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/*metabolism/ultrastructure ; *src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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