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Updated: Jun 8, 2026

A High-content Assay for Monitoring AMPA Receptor Trafficking
Published on: January 28, 2019
The ankyrin repeat-rich membrane spanning (ARMS)/Kidins220 scaffold protein is regulated by activity-dependent
Synphen H Wu1, Juan Carlos Arévalo, Veronika E Neubrand
1Molecular Neurobiology Program, Skirball Institute of Biomolecular Medicine, and Department of Physiology and Neuroscience, New York University School of Medicine, New York, New York 10016, USA. synphen.wu@nyumc.org
Abstract:
The expression of forms of synaptic plasticity, such as the phenomenon of long-term potentiation, requires the activity-dependent regulation of synaptic proteins and synapse composition. Here we show that ARMS (ankyrin repeat-rich membrane spanning protein)/Kidins220, a transmembrane scaffold molecule and BDNF TrkB substrate, is significantly reduced in hippocampal neurons after potassium chloride depolarization. The activity-dependent proteolysis of ARMS/Kidins220 was found to occur through calpain, a calcium-activated protease. Moreover, hippocampal long-term potentiation in ARMS/Kidins220(+/-) mice was enhanced, and inhibition of calpain in these mice reversed these effects. These results provide an explanation for a role for the ARMS/Kidins220 protein in synaptic plasticity events and suggest that the levels of ARMS/Kidins220 can be regulated by neuronal activity and calpain action to influence synaptic function.
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