Doc2 supports spontaneous synaptic transmission by a Ca(2+)-independent mechanism

Neuron. 2011 Apr 28;70(2):244-51. doi: 10.1016/j.neuron.2011.03.011.

Abstract

Two families of Ca(2+)-binding proteins have been proposed as Ca(2+) sensors for spontaneous release: synaptotagmins and Doc2s, with the intriguing possibility that Doc2s may represent high-affinity Ca(2+) sensors that are activated by deletion of synaptotagmins, thereby accounting for the increased spontaneous release in synaptotagmin-deficient synapses. Here, we use an shRNA-dependent quadruple knockdown of all four Ca(2+)-binding proteins of the Doc2 family to confirm that Doc2-deficient synapses exhibit a marked decrease in the frequency of spontaneous release events. Knockdown of Doc2s in synaptotagmin-1-deficient synapses, however, failed to reduce either the increased spontaneous release or the decreased evoked release of these synapses, suggesting that Doc2s do not constitute Ca(2+) sensors for asynchronous release. Moreover, rescue experiments revealed that the decrease in spontaneous release induced by the Doc2 knockdown in wild-type synapses is fully reversed by mutant Doc2B lacking Ca(2+)-binding sites. Thus, our data suggest that Doc2s are modulators of spontaneous synaptic transmission that act by a Ca(2+)-independent mechanism.

Publication types

  • Research Support, American Recovery and Reinvestment Act
  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Animals, Newborn
  • Biophysics
  • Calcium / metabolism*
  • Calcium-Binding Proteins / deficiency
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / physiology*
  • Cells, Cultured
  • Cerebral Cortex / cytology
  • Humans
  • Membrane Proteins / deficiency
  • Mice
  • Mice, Knockout
  • Mutagenesis, Site-Directed / methods
  • Mutation / physiology
  • Nerve Tissue Proteins / deficiency
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Nerve Tissue Proteins / physiology*
  • Neurons / drug effects
  • Neurons / physiology*
  • Patch-Clamp Techniques / methods
  • RNA Interference / physiology
  • Synaptic Transmission / drug effects
  • Synaptic Transmission / physiology*
  • Transfection
  • Vesicular Transport Proteins

Substances

  • Calcium-Binding Proteins
  • Doc2b protein, mouse
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Sytl1 protein, mouse
  • Vesicular Transport Proteins
  • rabphilin protein, mouse
  • Calcium