title: Stability of active zone components at the photoreceptor ribbon complex.
abstract: OBJECTIVE
  Photoreceptor ribbon synapses translate light-dependent changes of membrane potential into graded transmitter release over several orders of magnitude in intensity. A specialized organelle at the active zone--the synaptic ribbon--is a key player in this process, and it is well known that the ribbon undergoes illumination and thus activity-dependent structural changes. However, the molecular basis for these changes is unknown. The aim of this study was to correlate the known ultrastructural ribbon changes to the distribution of proteins of the presynaptic ribbon complex.
  
  
  METHODS
  In an in vitro assay, two distinct structural ribbon states--club-shaped and spherical-shaped--were enriched and the distribution of presynaptic proteins at the rod photoreceptor ribbon complex was analyzed with immunocytochemistry and light and electron microscopy.
  
  
  RESULTS
  We show that structural changes of the ribbon correlate with the redistribution of selected presynaptic proteins. The disassembly of the ribbon complex seems to be a multistep process, which starts with the removal of spherical ribbon material while arciform density and active zone plasma membrane proteins remain largely unchanged at their synaptic location. Only later, in a second phase following the removal of ribbon material, the arciform density and plasma membrane proteins are redistributed from their synaptic localization and active zones disappear.
  
  
  CONCLUSIONS
  The results of our study show that photoreceptor ribbon and arciform density/plasma membrane components might be influenced differentially by activity-driven processes, thus providing a molecular basis for further investigation of regulatory and adaptive processes in photoreceptor ribbon synaptic transmission.
authors.affiliation: Department of Biology, Animal Physiology, University of Erlangen-Nuremberg, Erlangen, Germany.
authors.forename: Hanna
authors.initials: H
authors.lastname: Regus-Leidig
authors.forename: Dana
authors.initials: D
authors.lastname: Specht
authors.forename: Susanne
authors.initials: S
authors.lastname: Tom Dieck
authors.forename: Johann Helmut
authors.initials: JH
authors.lastname: Brandstätter
mesh_terms: D000429:Alcohol Oxidoreductases; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D056970:Co-Repressor Proteins; D004268:DNA-Binding Proteins / Q000378:metabolism; D004533:Egtazic Acid / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D020419:Photoreceptor Cells, Vertebrate / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D017948:Retinal Rod Photoreceptor Cells / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D013569:Synapses / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: C498441:Bsn protein, mouse; D056970:Co-Repressor Proteins; D004268:DNA-Binding Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D004533:Egtazic Acid; D000429:Alcohol Oxidoreductases; C111341:Ctbp2 protein, mouse