Synaptic plasticity: Ups and downs of cerebellar plasticity

  title={Synaptic plasticity: Ups and downs of cerebellar plasticity},
  author={Suzanne J. Farley},
  journal={Nature Reviews Neuroscience},
  • S. Farley
  • Published 1 February 2004
  • Biology
  • Nature Reviews Neuroscience
NATURE REVIEWS | NEUROSCIENCE VOLUME 5 | FEBRUARY 2004 | 85 Among the changes in cerebellar synaptic efficacy that are thought to underlie motor learning, the best-studied is long-term depression (LTD). More than 20 years of intensive research attest to the complexity of this phenomenon, which is modulated by at least 30 interacting molecules. New data on one of these modulators — protein phosphatase-2A (PP-2A) — published in the Proceedings of the National Academy of Sciences bring us closer… 
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Protein phosphatase 2A inhibition induces cerebellar long-term depression and declustering of synaptic AMPA receptor.

It is reported that protein phosphatase 2A (PP-2A) plays a specific role in controlling synaptic strength and clustering of AMPARs at synapses between granule cells and Purkinje cells.

The molecular organization of cerebellar long-term depression

  • Masao Ito
  • Biology
    Nature Reviews Neuroscience
  • 2002
More than 30 molecules involved in the induction of long-term depression — a unique form of synaptic plasticity in the cerebellum — are reviewed, defining their roles as mediators or modulators, coincidence detectors or components of a self-regenerating circuit, and showing how they are organized to form an efficient molecular machinery for LTD induction.

Reversing cerebellar long-term depression

Postsynaptically expressed form of cerebellar parallel fiber–Purkinje cell long-term potentiation is a true counterbalance to LTD mediated by coincidence of NO plus postsynaptic Ca2+ elevation, unlike presynaptic LTP mediated by cAMP.

Roles of serine/threonine phosphatases in hippocampel synaptic plasticity

The roles of serine/threonine phosphatases in synaptic plasticity are reviewed and it is become increasingly clear that phosphatase have an equally dynamic and critical role in the activity-dependent alterations of synaptic transmission.