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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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1
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. 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.

PMID:
20943655
PMCID:
PMC3003345
DOI:
10.1074/jbc.M110.171371
[Indexed for MEDLINE]
Free PMC Article
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