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The Journal of Neuroscience, February 23, 2005, 25(8):1914-1923; doi:10.1523/JNEUROSCI.4790-04.2005

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Cellular/Molecular
A Protein Phosphatase 2c-Ca²⁺ Channel Complex for Dephosphorylation of Neuronal Ca²⁺ Channels Phosphorylated by Protein Kinase C

Dongjun Li, Fushun Wang, Meizan Lai, Yuan Chen, and Ji-fang Zhang

Department of Physiology, Jefferson Medical College, Philadelphia, Pennsylvania 19107

Phosphorylation and dephosphorylation are primary means for rapid regulation of a variety of neuronal functions, such as membrane excitability, neurotransmitter release, and gene expression. Voltage-gated Ca²⁺ channels are targets for phosphorylation by a variety of second messengers through activation of different types of protein kinases (PKs). Protein phosphatases (PPs), like PKs, are equally important in regulating Ca²⁺ channels in neurons. However, much less is understood about whether and how a particular type of PP contributes to regulating neuronal Ca²⁺ channel activities. This is primarily because of the lack of specific inhibitors/activators for different types of PPs, particularly the PP2c family. The functional roles of PP2c and its substrates in the brain remain virtually unknown. During our yeast two-hybrid screening, PP2c was pulled out by both N- and P/Q-type Ca²⁺ channel C termini. This raised the possibility that PP2c might be associated with voltage-gated Ca²⁺ channels for regulation of the Ca²⁺ channel activity. Biochemical studies show that PP2c binds directly to neuronal Ca²⁺ channels forming a functional protein complex in vivo. PP2c, unlike PP1, PP2a and PP2b, is more effective in dephosphorylation of neuronal Ca²⁺ channels after their phosphorylation by PKC. In hippocampal neurons, disruption of the PP2c-Ca²⁺ channel interaction significantly enhances the response of Ca²⁺ channels to modulation by PKC. Thus, the PP2c-Ca²⁺ channel complex is responsible for rapid dephosphorylation of Ca²⁺ channels and may contribute to regulation of synaptic transmission in neurons.

Key words: voltage-gated calcium channels; modulation; protein kinases; protein phosphatases; signal transduction; synaptic transmission

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Received Nov 23, 2004; revised January 2, 2005; accepted January 5, 2005.

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