In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-07-28)
Abstract:
In the brain, cells called neurons transmit information along their length in the form of electrical signals. To generate electrical signals, ions move into and out of neurons through ion channel proteins – such as the KCNQ channel – in the surface of these cells, which open and close to control the electrical response of the neuron. Abnormally intense bursts of electrical activity from many neurons at once can cause seizures such as those experienced by people with epilepsy. A significant proportion of patients do not respond to current anti-seizure medications. Openers of KCNQ channels have emerged as a potential new class of anti-epileptic drugs. A better understanding of how KCNQ channels work, and how their opening by PIP 2 lipid signals is regulated, could help to develop more effective therapies for epilepsy. A process called methylation controls many biological tasks by changing the structure of key proteins inside cells. Although methylation occurs throughout the brain, its role in controlling how easily neurons are activated (a property known as “excitability”) remains unclear. Kim, Jeong, Kim, Jung et al. now show that a protein called Prmt1 methylates the KCNQ channels in mice, and that this methylation is essential for suppressing seizures. Mice born without the Prmt1 protein developed epileptic seizures and the KCNQ channels in their neurons featured a reduced level of methylation. However, increasing the amount of PIP 2 in these neurons restored their excitability back to normal levels. The methylation of KCNQ channel proteins increases their affinity for PIP2, which is critical to open KCNQ channels. Kim et al. propose that these “opening” controllers balance the action of known “closers” of KCNQ channels to maintain neurons in a healthy condition. In future, Kim et al. plan to investigate whether methylation affects the activity of other ion channels controlled by PIP 2 . Such experiments will complement a more widespread investigation into other ways in which the Prtmt1 protein may control the activity of neurons.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.17159.001
DOI:
10.7554/eLife.17159.002
DOI:
10.7554/eLife.17159.003
DOI:
10.7554/eLife.17159.004
DOI:
10.7554/eLife.17159.005
DOI:
10.7554/eLife.17159.006
DOI:
10.7554/eLife.17159.007
DOI:
10.7554/eLife.17159.008
DOI:
10.7554/eLife.17159.009
DOI:
10.7554/eLife.17159.010
DOI:
10.7554/eLife.17159.011
DOI:
10.7554/eLife.17159.012
DOI:
10.7554/eLife.17159.013
DOI:
10.7554/eLife.17159.014
DOI:
10.7554/eLife.17159.015
DOI:
10.7554/eLife.17159.016
DOI:
10.7554/eLife.17159.017
DOI:
10.7554/eLife.17159.018
DOI:
10.7554/eLife.17159.019
DOI:
10.7554/eLife.17159.020
DOI:
10.7554/eLife.17159.021
DOI:
10.7554/eLife.17159.022
DOI:
10.7554/eLife.17159.023
DOI:
10.7554/eLife.17159.024
DOI:
10.7554/eLife.17159.025
DOI:
10.7554/eLife.17159.026
DOI:
10.7554/eLife.17159.027
DOI:
10.7554/eLife.17159.028
DOI:
10.7554/eLife.17159.029
DOI:
10.7554/eLife.17159.030
DOI:
10.7554/eLife.17159.031
DOI:
10.7554/eLife.17159.032
DOI:
10.7554/eLife.17159.033
DOI:
10.7554/eLife.17159.034
DOI:
10.7554/eLife.17159.035
DOI:
10.7554/eLife.17159.036
DOI:
10.7554/eLife.17159.037
DOI:
10.7554/eLife.17159.038
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2016
detail.hit.zdb_id:
2687154-3