Selective saturation of slow endocytosis at a giant glutamatergic central synapse lacking dynamin 1

  1. Xuelin Lou,
  2. Summer Paradise,
  3. Shawn M. Ferguson, and
  4. Pietro De Camilli1
  1. Departments of Cell Biology and Neurobiology, Howard Hughes Medical Institute, Kavli Institute for Neuroscience, Program in Cellular Neuroscience, Neurodegeneration and Repair, Yale University School of Medicine, New Haven, CT 06510
  1. Contributed by Pietro De Camilli, September 25, 2008 (received for review August 18, 2008)

Abstract

Exocytosis of synaptic vesicles is rapidly followed by compensatory plasma membrane endocytosis. The efficiency of endocytosis varies with experimental conditions, but the molecular basis for this control remains poorly understood. Here, the function of dynamin 1, the neuron-specific member of a family of GTPases implicated in vesicle fission, was investigated with high temporal resolution via membrane capacitance measurements at the calyx of Held, a giant glutamatergic synapse. Endocytosis at dynamin 1 KO calyces was the same as in wild type after weak stimuli, consistent with the nearly normal ultrastructure of mutant synapses. However, following stronger stimuli, the speed of slow endocytosis, but not of other forms of endocytosis, failed to scale with the increased endocytic load. Thus, high level expression of dynamin 1 is essential to allow the slow, clathrin-mediated endocytosis, which accounts for the bulk of the endocytic response, to operate efficiently over a wide range of activity.

Footnotes

  • 1To whom correspondence should be addressed at:
    Department of Cell Biology, Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510.
    E-mail: pietro.decamilli{at}yale.edu
  • Author contributions: X.L., S.M.F., and P.D.C. designed research; X.L. and S.P. performed research; S.M.F. contributed new reagents/analytic tools; X.L., S.P., and P.D.C. analyzed data; and X.L. and P.D.C. wrote the paper.

  • The authors declare no conflict of interest.

  • This article contains supporting information online at www.pnas.org/cgi/content/full/0809621105/DCSupplemental.

  • Freely available online through the PNAS open access option.

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