Journal
NATURE NEUROSCIENCE
Volume 5, Issue 3, Pages 210-217Publisher
NATURE AMERICA INC
DOI: 10.1038/nn805
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Funding
- NATIONAL EYE INSTITUTE [R01EY008061] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [F32NS010645, R01NS022625] Funding Source: NIH RePORTER
- NEI NIH HHS [R01 EY08061, R01 EY008061] Funding Source: Medline
- NINDS NIH HHS [F32 NS010645, R01 NS22625, R01 NS022625, F32 NS10645] Funding Source: Medline
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Ca(v)2.1 channels, which mediate P/Q-type Ca2+ currents, undergo Ca2+/calmodulin (CaM) dependent inactivation and facilitation that can significantly alter synaptic efficacy. Here we report that the neuronal Ca2+-binding protein 1 (CaBP1) modulates Ca(v)2.1 channels in a manner that is markedly different from modulation by CaM. CaBP1 enhances inactivation, causes a depolarizing shift in the voltage dependence of activation, and does not support Ca2+-dependent facilitation of Ca(v)2.1 channels. These inhibitory effects of CaBP1 do not require Ca2+, but depend on the CaM-binding domain in the alpha(1) subunit of Ca(v)2.1 channels (alpha(1)2.1). CaBP1 binds to the CaM-binding domain, co-immunoprecipitates with alpha(1)2.1 from transfected cells and brain extracts, and colocalizes with alpha(1)2.1 in discrete microdomains of neurons in the hippocampus and cerebellum. Our results identify an interaction between Ca2+ channels and CaBP1 that may regulate Ca2+-dependent forms of synaptic plasticity by inhibiting Ca2+ influx into neurons.
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