From the most basic of nervous systems to the intricate circuits found within the human brain, a fundamental requirement of neuronal function is that it be malleable, altering its output based upon experience. A host of cellular proteins are recruited for this purpose, which themselves are regulated by protein phosphorylation. Over the past several decades, research has demonstrated that the Ca2+ and calmodulin-dependent protein phosphatase calcineurin (protein phosphatase 2B) is a critical regulator of a diverse array of proteins, leading to both short- and long-term effects on neuronal excitability and function. This review describes many of the influences of calcineurin on a variety of proteins, including ion channels, neurotransmitter receptors, enzymes, and transcription factors. Intriguingly, due to the bi-directional influences of Ca2+ and calmodulin on calcineurin activity, the strength and duration of particular stimulations may cause apparently antagonistic functions of calcineurin to work in concert.
|Original language||English (US)|
|Number of pages||13|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 28 2003|
Bibliographical noteFunding Information:
R.D.G. is supported by NIH training Grant DA07234. R.L.D. is supported by a Duke University post-doctoral fellowship. P.G.M. is supported by NIH Grant NS41302 and the Whitehall Foundation. The authors would like to thank Jeremy Bergsman, Karl Deisseroth, Geoffrey Pitt, Mark Thomas, and Ann Isaksen for the critical reading of the manuscript.
- Inhibitor 1
- Protein phosphatase 2B