scholarly journals Several Structural Domains Contribute to the Regulation of N-type Calcium Channel Inactivation by the β3Subunit

2003 ◽  
Vol 279 (5) ◽  
pp. 3793-3800 ◽  
Author(s):  
Stephanie C. Stotz ◽  
Wendy Barr ◽  
John E. McRory ◽  
Lina Chen ◽  
Scott E. Jarvis ◽  
...  
Keyword(s):  
Calcium Channel ◽  
Structural Domains ◽  
Channel Inactivation ◽  
Calcium Channel Inactivation

scholarly journals Molecular Structures Involved in L-type Calcium Channel Inactivation

1997 ◽  
Vol 272 (6) ◽  
pp. 3560-3566 ◽  
Author(s):  
Nikolai M. Soldatov ◽  
Roger D. Zühlke ◽  
Alexandre Bouron ◽  
Harald Reuter
Keyword(s):  
Calcium Channel ◽  
Molecular Structures ◽  
Channel Inactivation ◽  
Calcium Channel Inactivation

scholarly journals Robust switches in thalamic network activity require a timescale separation between sodium and T-type calcium channel activations

2020 ◽  
Author(s):  
Kathleen Jacquerie ◽  
Guillaume Drion
Keyword(s):  
Synaptic Plasticity ◽  
Calcium Channel ◽  
Network Activity ◽  
Channel Activation ◽  
Channel Inactivation ◽  
Calcium Channel Inactivation ◽  
Target Neuron ◽  
Sodium Channel Activation ◽  
Brain States

AbstractSwitches in brain states, synaptic plasticity and neuromodulation are fundamental processes in our brain that take place concomitantly across several spatial and timescales. All these processes target neuron intrinsic properties and connectivity to achieve specific physiological goals, raising the question of how they can operate without interfering with each other. Here, we highlight the central importance of a timescale separation in the activation of sodium and T-type calcium channels to sustain robust switches in brain states in thalamic neurons that are compatible with synaptic plasticity and neuromodulation. We quantify the role of this timescale separation by comparing the robustness of rhythms of six published conductance-based models at the cellular, circuit and network levels. We show that robust rhythm generation requires a T-type calcium channel activation whose kinetics are situated between sodium channel activation and T-type calcium channel inactivation in all models despite their quantitative differences.

scholarly journals Molecular Determinants of Cav1.2 Calcium Channel Inactivation

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Nikolai M. Soldatov
Keyword(s):  
Calcium Channel ◽  
Neuronal Plasticity ◽  
Calcium Current ◽  
Cellular Functions ◽  
Current Decay ◽  
Vascular Muscle ◽  
Channel Inactivation ◽  
Calcium Channel Inactivation ◽  
Benefit Function ◽  
Molecular Determinants

Voltage-gated L-type Cav1.2 calcium channels couple membrane depolarization to transient increase in cytoplasmic free Ca2+ concentration that initiates a number of essential cellular functions including cardiac and vascular muscle contraction, gene expression, neuronal plasticity, and exocytosis. Inactivation or spontaneous termination of the calcium current through Cav1.2 is a critical step in regulation of these processes. The pathophysiological significance of this process is manifested in hypertension, heart failure, arrhythmia, and a number of other diseases where acceleration of the calcium current decay should present a benefit function. The central issue of this paper is the inactivation of the Cav1.2 calcium channel mediated by multiple determinants.

Identification of a second region of the beta-subunit involved in regulation of calcium channel inactivation

1996 ◽  
Vol 271 (5) ◽  
pp. C1539-C1545 ◽  
Author(s):  
N. Qin ◽  
R. Olcese ◽  
J. Zhou ◽  
O. A. Cabello ◽  
L. Birnbaumer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Calcium Channel ◽  
Splice Variants ◽  
Terminal Segment ◽  
Beta Subunit ◽  
Beta Subunits ◽  
High Sequence Identity ◽  
Channel Inactivation ◽  
Calcium Channel Inactivation ◽  
Common Effect

Previous studies have shown that NH2 termini of the type 1 and 2 beta-subunits modulate the rate at which the neuronal alpha 1E calcium channel inactivates in response to voltage and that they do so independently of their common effect to stimulate activation by voltage (R. Olcese, N. Qin, T. Schneider, A. Neely, X. Wei, E. Stefani, and L. Birnbaumer, Neuron 13: 1433-1438, 1994). By constructing NH2-terminal deletions of several splice variants of beta-subunits, we have now found differences in the way they affect the rate of alpha 1E inactivation that lead us to identify a second domain that also regulates the rate of voltage-induced inactivation of the Ca2+ channel. This second domain, named segment 3, lies between two regions of high-sequence identity between all known beta-subunits and exists in two lengths (long and short), each encoded in a separate exon. Beta-Subunits with the longer 45- to 53-amino acid version cause the channel to inactivate more slowly than subunits with the shorter 7-amino acid version. As is the case for the NH2 terminus, the segment 3 does not affect the regulation of channel activation by the beta-subunit. In addition, the effect of the NH2-terminal segment prevails over that of the internal segment. This raises the possibility that phosphorylation, other types of posttranslational modification, or interaction with other auxiliary calcium channel subunits may be necessary to unmask the regulatory effect of the internal segment.

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