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Updated: Jun 5, 2026

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
CALM, a clathrin assembly protein, influences cell surface GluR2 abundance
Asaff Harel1, Mark P Mattson, Pamela J Yao
1Laboratory of Neurosciences, National Institute on Aging Intramural Research Program, NIH, 251 Bayview Boulevard, Baltimore, MD 21224, USA.
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.
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