@misc{10481/86479,
year = {2010},
url = {https://hdl.handle.net/10481/86479},
abstract = {The expression of forms of synaptic plasticity, such as thephenomenon 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 ex planation for a role for the ARMS/Kidins220 protein in synap tic plasticity events and suggest that the levels of ARMS/Kidins220 can be regulated by neuronal activity and calpain action to influence synaptic function.},
organization = {National Institutes of
Health Grants NS21072 and HD23315 and NS049442},
organization = {Medical Scientist Training
Program},
organization = {Marie Curie International Reintegration Grant
within the 7th European Community Framework Programme},
publisher = {The American Society for Biochemistry and Molecular Biology},
keywords = {ARMS},
keywords = {Kidins220},
keywords = {Synaptic plasticity},
keywords = {Calpain proteolysis},
title = {The Ankyrin Repeat-rich Membrane Spanning (ARMS)/Kidins220 Scaffold Protein Is Regulated by Activity-dependent Calpain Proteolysis and Modulates Synaptic Plasticity},
doi = {10.1074/jbc.M110.171371},
author = {Wu, Synphen H and Arévalo, Juan Carlos and Neubrand, Veronika Elisabeth and Zhang, Hong and Arrancio, Ottavio and Chao, Moses V},
}