Neuronal activity dephosphorylate and translocate Kv2.1 ion channel:

04 Nature: "Regulation of ion channel localization and phosphorylation by neuronal" activityhttp://www.nature.com/neuro/journal/v7/n7/full/nn1260.html
Voltage-dependent Kv2.1 K⁺ channels, which mediate delayed rectifier Kv currents (I_K), are expressed in large clusters on the somata and dendrites of principal pyramidal neurons, where they regulate neuronal excitability.

Very good review: "Localization of Voltage-Gated Ion Channels IN Mammalian Brain" in Annual review of physiology
http://arjournals.annualreviews.org/doi/full/10.1146/annurev.physiol.66.032102.113328?cookieSet=1

Should be interesting to know

Title: Regulation of the timing of MNTB neurons by short-term and long-term modulation of potassium channels

I know some families of potassium channel are important in auditory function. Especially the ones in the hair cells. But this is something I didn't know.

http://www.sciencedirect.com.ezproxy.hsclib.sunysb.edu/science?_ob=ArticleURL&_udi=B6T73-4FXV7BJ-3&_user=334567&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000017318&_version=1&_urlVersion=0&_userid=334567&md5=bb2dd706f5fc02dee27cde9d9097e1ed

Abstract

The firing patterns of neurons in central auditory pathways encode specific features of sound stimuli, such as frequency, intensity and localization in space. The generation of the appropriate pattern depends, to a major extent, on the properties of the voltage-dependent potassium channels in these neurons. The mammalian auditory pathways that compute the direction of a sound source are located in the brainstem and include the connection from bushy cells in the anteroventral cochlear nucleus (AVCN) to the principal neurons of the medial nucleus of the trapezoid body (MNTB). To preserve the fidelity of timing of action potentials that is required for sound localization, these neurons express several types of potassium channels, including the Kv3 and Kv1 families of voltage-dependent channels and the Slick and Slack sodium-dependent channels. These channels determine the pattern of action potentials and the amount of neurotransmitter released during repeated stimulation. The amplitude of currents carried by one of these channels, the Kv3.1b channel, is regulated in the short term by protein phosphorylation, and in the long term, by changes in gene expression, such that the intrinsic excitability of the neurons is constantly being regulated by the ambient auditory environment.

Potassium channel -Kv2.1

http://www.sciencedirect.com.ezproxy.hsclib.sunysb.edu/science?_ob=ArticleURL&_udi=B6W81-4GC1R5J-3&_user=334567&_coverDate=10%2F31%2F2005&_rdoc=1&_fmt=&_orig=search&_sort=d&view=c&_acct=C000017318&_version=1&_urlVersion=0&_userid=334567&md5=5c696ee8356d440545693b7d60914a00
The function of Kv channels can be described in simple terms using the biophysical properties that determine
1. at which membrane potentials the channels will open,
2. how quickly they open in response to the membrane potential achieving these potentials,
3. if open how long they remain so, and
4. when open at what rate do they allow flux of K+ across the membrane (MacKinnon, 2003). While these inherent biophysical properties are clearly encoded within the primary structure of the particular channel subtype, they can also be modified through post-translational events including covalent modifications (usually phosphorylation) and non-covalent protein–protein interactions (Jonas and Kaczmarek, 1996 and Yi et al., 2001). The biophysical characteristics can also be dramatically modified pharmacologically, a fact that serves as the basis for a diverse array of promising therapeutics (Wickenden, 2002).

http://www.sciencedirect.com.ezproxy.hsclib.sunysb.edu/science?_ob=ArticleURL&_udi=B6T36-49PR9Y1-5&_user=334567&_coverDate=11%2F27%2F2003&_fmt=full&_orig=search&_cdi=4938&view=c&_acct=C000017318&_version=1&_urlVersion=0&_userid=334567&md5=2fd40848628da5e0ffe33c8700ec2db1&ref=full
Therefore, the different kinds of K+ channels open in response to different stimuli: a change in the intracellular Ca2+ concentration, the level of certain G-protein subunits in the cell, or the value of the membrane voltage. Underneath this diversity in gating function, K+ channels have diverse structural domains attached in a modular fashion to the conserved pore unit. Ligand-gated K+ channels typically have cytoplasmic or extracellular domains for binding ligands. Voltage-gated K+ channels have integral membrane domains for sensing voltage differences.