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J Biol Chem. 2010 Dec 24;285(52):40472-8. doi: 10.1074/jbc.M110.171371. Epub 2010 Oct 13.

The ankyrin repeat-rich membrane spanning (ARMS)/Kidins220 scaffold protein is regulated by activity-dependent calpain proteolysis and modulates synaptic plasticity.

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Molecular 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.


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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