The synaptic vesicle protein CSP alpha prevents presynaptic degeneration

Neuron. 2004 Apr 22;42(2):237-51. doi: 10.1016/s0896-6273(04)00190-4.

Abstract

Cysteine string protein alpha (CSPalpha)--an abundant synaptic vesicle protein that contains a DNA-J domain characteristic of Hsp40 chaperones--is thought to regulate Ca2+ channels and/or synaptic vesicle exocytosis. We now show that, in young mice, deletion of CSPalpha does not impair survival and causes no significant changes in presynaptic Ca2+ currents or synaptic vesicle exocytosis as measured in the Calyx of Held synapse. At 2-4 weeks of age, however, CSPalpha-deficient mice develop a progressive, fatal sensorimotor disorder. The neuromuscular junctions and Calyx synapses of CSPalpha-deficient mice exhibit increasing neurodegenerative changes, synaptic transmission becomes severely impaired, and the mutant mice die at approximately 2 months of age. Our data suggest that CSPalpha is not essential for the normal operation of Ca2+ channels or exocytosis but acts as a presynaptic chaperone that maintains continued synaptic function, raising the possibility that enhanced CSPalpha function could attenuate neurodegenerative diseases.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Animals, Newborn
  • Brain / metabolism
  • Brain / ultrastructure
  • HSP40 Heat-Shock Proteins
  • Membrane Proteins / biosynthesis*
  • Membrane Proteins / deficiency
  • Membrane Proteins / genetics
  • Mice
  • Mice, Knockout
  • Nerve Degeneration / genetics
  • Nerve Degeneration / metabolism*
  • Neuromuscular Junction / genetics
  • Neuromuscular Junction / metabolism
  • Neuromuscular Junction / ultrastructure
  • Presynaptic Terminals / metabolism*
  • Presynaptic Terminals / ultrastructure
  • Synaptic Vesicles / genetics
  • Synaptic Vesicles / metabolism*
  • Synaptic Vesicles / ultrastructure

Substances

  • HSP40 Heat-Shock Proteins
  • Membrane Proteins
  • cysteine string protein