Bi-directional control of motor neuron dendrite remodeling by the calcium permeability of AMPA receptors

Goo Bo Jeong, Markus Werner, Valeswara Rao Gazula, Takayuki Itoh, Melinda Roberts, Samuel David, Bryan Pfister, Akiva Cohen, Rachael L. Neve, Michael Hollmann, Robert Kalb

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Motor neurons express particularly high levels of the AMPA receptor subunit GluR1(Q)flip (GluR1(Q)i) during the period in early postnatal life when their dendritic tree grows and becomes more branched. To investigate how GluR1-containing AMPA receptors contribute to dendrite morphogenesis, we characterized a mutant form of GluR1 (containing a histidine in the Q/R editing site) with unique electrophysiological properties. Most notably, AMPA receptors assembled from GluR1(H)i display less calcium permeability than AMPA receptors assembled from GluR1(Q)i. Expression of GluR1(Q)i in vivo or in vitro led to an increase in dendrite branching with no net change in the overall tree size while GluR1(H)i led to a loss of branches and a net reduction in overall tree size. GluR1(H)i-dependent dendrite atrophy is mediated by protein phosphatase 2B. The results suggest that the electrophysiological properties of cell surface AMPA receptors, specifically their permeability to calcium, can be a central determinant of whether the dendrites undergo activity-dependent branching or atrophy.

Original languageEnglish (US)
Pages (from-to)299-314
Number of pages16
JournalMolecular and Cellular Neuroscience
Volume32
Issue number3
DOIs
StatePublished - Jul 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Keywords

  • Activity-dependent plasticity
  • Calcium
  • GluR1
  • Herpes Simplex Virus
  • Spinal cord
  • Transgene, calcineurin

Fingerprint

Dive into the research topics of 'Bi-directional control of motor neuron dendrite remodeling by the calcium permeability of AMPA receptors'. Together they form a unique fingerprint.

Cite this