| Literature DB >> 33909214 |
Seok Kyo Shin1, Hai Ying Li2, Kun Cho3, Young Wuk Cho1, Jung-Ha Lee2, Kang-Sik Park4.
Abstract
Cav1.2 channel phosphorylation plays an important role in regulating neuronal plasticity by action potential-dependent Ca2+ entry. Most studies of Cav1.2 regulation by phosphorylation have been reported in heart and muscles. Here, we identified phosphorylation sites of neuronal Cav1.2 channel protein purified from rat brain using mass spectrometry. The functional characterization of these phosphorylation sites showed altered voltage-dependent biophysical properties of the channel, without affecting current density. These results show that neuronal Cav1.2 channel is regulated by phosphorylation in a complex mechanism involving multiple phosphorylation sites.Entities:
Keywords: Cav1.2; Mass spectrometry; Neuron; Phosphorylation
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Year: 2021 PMID: 33909214 DOI: 10.1007/s10571-021-01095-2
Source DB: PubMed Journal: Cell Mol Neurobiol ISSN: 0272-4340 Impact factor: 4.231