| First Author | Wu SH | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 52 | Pages | 40472-8 |
| PubMed ID | 20943655 | Mgi Jnum | J:167592 |
| Mgi Id | MGI:4868575 | Doi | 10.1074/jbc.M110.171371 |
| Citation | Wu SH, et al. (2010) The ankyrin repeat-rich membrane spanning (ARMS)/Kidins220 scaffold protein is regulated by activity-dependent calpain proteolysis and modulates synaptic plasticity. J Biol Chem 285(52):40472-8 |
| abstractText | 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. |
