GluR1 controls dendrite growth through its binding partner, SAP97

Weiguo Zhou, Lei Zhang, Xiong Guoxiang, Jelena Mojsilovic-Petrovic, Kogo Takamaya, Rita Sattler, Richard Huganir, Robert Kalb

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


Activity-dependent dendrite elaboration influences the pattern of interneuronal connectivity and network function. In the present study, we examined the mechanism by which the GluR1 subunit of AMPA receptors controls dendrite morphogenesis. GluR1 binds to SAP97, a scaffolding protein that is a component of the postsynaptic density, via its C-terminal 7 aa. We find that elimination of this interaction in vitro or in vivo (by deleting the C-terminal 7 aa of GluR1, GluR1Δ7) does not influence trafficking, processing, or cell surface GluR1 expression but does prevent translocation of SAP97 from the cytosol to membranes. GluR1 and SAP97 together at the plasma membrane promotes dendrite branching in an activity-dependent manner, although this does not require physical association. Our findings suggest that the C-terminal 7 aa of GluR1 are essential for bringing SAP97 to the plasma membrane, where it acts to translate the activity of AMPA receptors into dendrite growth.

Original languageEnglish (US)
Pages (from-to)10220-10233
Number of pages14
JournalJournal of Neuroscience
Issue number41
StatePublished - Oct 8 2008


  • Motor neurons
  • Postsynaptic density
  • Scaffold protein
  • Spinal cord
  • Synaptic activity
  • Trafficking

ASJC Scopus subject areas

  • Neuroscience(all)


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