Journal article
Ca2+-Dependent Facilitation of Cav1.3 Ca2+ Channels by Densin and Ca2+/Calmodulin-Dependent Protein Kinase II
The Journal of neuroscience, Vol.30(15), pp.5125-5135
04/14/2010
DOI: 10.1523/JNEUROSCI.4367-09.2010
PMCID: PMC2990970
PMID: 20392935
Abstract
Ca
v
1 (L-type) channels and calmodulin-dependent protein kinase II (CaMKII) are key regulators of Ca
2+
signaling in neurons. CaMKII directly potentiates the activity of Ca
v
1.2 and Ca
v
1.3 channels, but the underlying molecular mechanisms are incompletely understood. Here, we report that the CaMKII-associated protein densin is required for Ca
2+
-dependent facilitation of Ca
v
1.3 channels. While neither CaMKII nor densin independently affects Ca
v
1.3 properties in transfected HEK293T cells, the two together augment Ca
v
1.3 Ca
2+
currents during repetitive, but not sustained, depolarizing stimuli. Facilitation requires Ca
2+
, CaMKII activation, and its association with densin, as well as densin binding to the Ca
v
1.3 α
1
subunit C-terminal domain. Ca
v
1.3 channels and densin are targeted to dendritic spines in neurons and form a complex with CaMKII in the brain. Our results demonstrate a novel mechanism for Ca
2+
-dependent facilitation that may intensify postsynaptic Ca
2+
signals during high-frequency stimulation.
Details
- Title: Subtitle
- Ca2+-Dependent Facilitation of Cav1.3 Ca2+ Channels by Densin and Ca2+/Calmodulin-Dependent Protein Kinase II
- Creators
- Meagan A Jenkins - Department of Pharmacology, Emory University, Atlanta, Georgia 30322Carl J Christel - Departments of Molecular Physiology and Biophysics andYuxia Jiao - Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232, andSunday Abiria - Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232, andKristin Y Kim - Departments of Molecular Physiology and Biophysics andYuriy M Usachev - Pharmacology, University of Iowa, Iowa City, Iowa 52242Gerald J Obermair - Department of Physiology and Medical Physics, Innsbruck Medical University, A-6020 Innsbruck, AustriaRoger J Colbran - Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37232, andAmy Lee - Departments of Molecular Physiology and Biophysics and
- Resource Type
- Journal article
- Publication Details
- The Journal of neuroscience, Vol.30(15), pp.5125-5135
- Publisher
- Society for Neuroscience
- DOI
- 10.1523/JNEUROSCI.4367-09.2010
- PMID
- 20392935
- PMCID
- PMC2990970
- ISSN
- 0270-6474
- eISSN
- 1529-2401
- Language
- English
- Date published
- 04/14/2010
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Anesthesia; Fraternal Order of Eagles Diabetes Research Center; Neuroscience and Pharmacology
- Record Identifier
- 9984070606302771
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