CALM, A clathrin assembly protein, influences cell surface GluR2 abundance

Asaff Harel, Mark P. Mattson, Pamela J. Yao

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

The clathrin assembly protein, CALM, promotes the assembly of clathrin-coated vesicles. In a previous study, we showed that CALM controls the level of the synaptic vesicle protein VAMP2 at the plasma membrane by regulating VAMP2 endocytosis. Here, we provide evidence that CALM also influences the cell surface level of the AMPA receptor subunit GluR2. Although mechanistic details as well as the physiological relevance of CALM and GluR2 in the neuron have yet to be established, CALM-mediated trafficking could function as a component of a dedicated system for controlling postsynaptic abundance of GluR2.

Original languageEnglish (US)
Pages (from-to)88-90
Number of pages3
JournalNeuroMolecular Medicine
Volume13
Issue number1
DOIs
StatePublished - Mar 2011
Externally publishedYes

Keywords

  • AMPA receptor
  • AP180
  • Bungarotoxin binding site
  • CALM
  • Clathrin
  • GluR2

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Molecular Medicine
  • Neurology

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