Intersectin Is a Negative Regulator of Dynamin Recruitment to the Synaptic Endocytic Zone in the Central Synapse

Intersectin is a multidomain dynamin-binding protein implicated in numerous functions in the nervous system, including synapse formation and endocytosis. Here, we demonstrate that during neurotransmitter release in the central synapse, intersectin, like its binding partner dynamin, is redistributed...

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Bibliographic Details
Published in:The Journal of neuroscience 2007-01, Vol.27 (2), p.379-390
Main Authors: Evergren, Emma, Gad, Helge, Walther, Kristin, Sundborger, Anna, Tomilin, Nikolay, Shupliakov, Oleg
Format: Article
Language:English
Subjects:
Adaptor Proteins, Vesicular Transport - physiology
Amino Acid Sequence
Animals
Dynamins - antagonists & inhibitors
Dynamins - metabolism
Endocytosis - physiology
Endosomes - physiology
Endosomes - ultrastructure
Lampreys
Molecular Sequence Data
Neural Inhibition - physiology
Synapses - physiology
Synapses - ultrastructure
Synaptic Vesicles - physiology
Synaptic Vesicles - ultrastructure
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Summary:Intersectin is a multidomain dynamin-binding protein implicated in numerous functions in the nervous system, including synapse formation and endocytosis. Here, we demonstrate that during neurotransmitter release in the central synapse, intersectin, like its binding partner dynamin, is redistributed from the synaptic vesicle pool to the periactive zone. Acute perturbation of the intersectin-dynamin interaction by microinjection of either intersectin antibodies or Src homology 3 (SH3) domains inhibited endocytosis at the fission step. Although the morphological effects induced by the different reagents were similar, antibody injections resulted in a dramatic increase in dynamin immunoreactivity around coated pits and at constricted necks, whereas synapses microinjected with the GST (glutathione S-transferase)-SH3C domain displayed reduced amounts of dynamin in the neck region. Our data suggest that intersectin controls the amount of dynamin released from the synaptic vesicle cluster to the periactive zone and that it may regulate fission of clathrin-coated intermediates.
ISSN:0270-6474
1529-2401
DOI:10.1523/JNEUROSCI.4683-06.2007