Calmodulin Is a Functional Regulator of Cav1.4 L-type Ca Channels*
نویسندگان
چکیده
Kristina Griessmeier, Hartmut Cuny, Katrin Rötzer, Oliver Griesbeck, Hartmann Harz, Martin Biel, and Christian Wahl-Schott From the Center for Integrated Protein Science (CIPS-M) and Zentrum für Pharmaforschung, Department Pharmazie, Ludwig-Maximilians-Universität München, D-81377 München, the Max Planck Institute of Neurobiology, D-82152 Martinsried, and the BioImaging Zentrum, Ludwig-Maximilians-Universität München, D-81377 München, Germany
منابع مشابه
Protein kinase A modulation of CaV1.4 calcium channels
The regulation of L-type Ca(2+) channels by protein kinase A (PKA) represents a crucial element within cardiac, skeletal muscle and neurological systems. Although much work has been done to understand this regulation in cardiac CaV1.2 Ca(2+) channels, relatively little is known about the closely related CaV1.4 L-type Ca(2+) channels, which feature prominently in the visual system. Here we find ...
متن کاملCalmodulin is a functional regulator of Cav1.4 L-type Ca2+ channels.
Cav1.4 channels are unique among the high voltage-activated Ca2+ channel family because they completely lack Ca2+-dependent inactivation and display very slow voltage-dependent inactivation. Both properties are of crucial importance in ribbon synapses of retinal photoreceptors and bipolar cells, where sustained Ca2+ influx through Cav1.4 channels is required to couple slow graded changes of the...
متن کاملStructural insights into activation of the retinal L-type Ca²⁺ channel (Cav1.4) by Ca²⁺-binding protein 4 (CaBP4).
CaBP4 modulates Ca(2+)-dependent activity of L-type voltage-gated Ca(2+) channels (Cav1.4) in retinal photoreceptor cells. Mg(2+) binds to the first and third EF-hands (EF1 and EF3), and Ca(2+) binds to EF1, EF3, and EF4 of CaBP4. Here we present NMR structures of CaBP4 in both Mg(2+)-bound and Ca(2+)-bound states and model the CaBP4 structural interaction with Cav1.4. CaBP4 contains an unstruc...
متن کاملSwitching off calcium-dependent inactivation in L-type calcium channels by an autoinhibitory domain.
The retinal L-type Ca2+ channel Cav1.4 is distinguished from all other members of the high voltage-activated (HVA) Ca2+ channel family by lacking Ca2+-calmodulin-dependent inactivation. In synaptic terminals of photoreceptors and bipolar cells, this feature is essential to translate graded membrane depolarizations into sustained Ca2+ influx and tonic glutamate release. The sequences conferring ...
متن کاملGain-of-function nature of Cav1.4 L-type calcium channels alters firing properties of mouse retinal ganglion cells
Proper function of Cav1.4 L-type calcium channels is crucial for neurotransmitter release in the retina. Our understanding about how different levels of Cav1.4 channel activity affect retinal function is still limited. In the gain-of-function mouse model Cav1.4-IT we expected a reduction in the photoreceptor dynamic range but still transmission toward retinal ganglion cells. A fraction of Cav1....
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تاریخ انتشار 2009