Alternate Splicing in the Cytosolic II–III Loop and the Carboxy Terminus of Human E-type Voltage-Gated Ca2+ Channels: Electrophysiological Characterization of Isoforms

@article{Pereverzev2002AlternateSI,
  title={Alternate Splicing in the Cytosolic II–III Loop and the Carboxy Terminus of Human E-type Voltage-Gated Ca2+ Channels: Electrophysiological Characterization of Isoforms},
  author={A. Pereverzev and J{\'e}r{\^o}me Leroy and Andreas Krieger and Claire O. Mal{\'e}cot and Jürgen Hescheler and Gabriele Pfitzer and Udo Klöckner and Toni Schneider},
  journal={Molecular and Cellular Neuroscience},
  year={2002},
  volume={21},
  pages={352-365}
}
There is growing evidence that Ca(v)2.3 (alpha1E, E-type) transcripts may encode the ion-conducting subunit of a subclass of R-type Ca(2+) channels, a heterogeneous group of channels by definition resistant to blockers of L-, N-, and P/Q-type Ca(2+) channels. To understand whether splice variation of Ca(v)2.3 contributes to the divergence of R-type channels, individual variants of Ca(v)2.3 were constructed and expressed in HEK-293 cells. With Ba(2+) as charge carrier, the tested biophysical… Expand
The C-terminus of human Ca(v)2.3 voltage-gated calcium channel interacts with alternatively spliced calmodulin-2 expressed in two human cell lines.
TLDR
To analyze Ca(2+) mediated modulation of cellular processes more in detail, protein partners of the carboxy terminal tail of Ca(v)2.3 were identified by yeast-2-hybrid screening, leading in two human cell lines to the detection of a novel, extended and rarely occurring splice variant of calmodulin-2 (CaM-2), called CaM- 2-extended (Ca m2-ext). Expand
The Molecular Chaperone hsp70 Interacts with the Cytosolic II-III Loop of the Cav2.3 E-type Voltagegated Ca2+ Channel
TLDR
To understandCa2+ and phorbol ester mediated activation of Cav2.3 Ca2+ channels, protein interaction partners of the II-III loop were identified and the molecular chaperone hsp70, which is known to interact with PKC, was identified as a novel functional interaction partner. Expand
Interaction of recombinant and native Cav2.3 E-/R-type voltage-gated Ca2+ channels with the molecular chaperone Hsp70
Correspondence: Toni schneider institute of neurophysiology, University of Cologne, Robert-Koch-str 39, D-50931 Köln, germany Tel +49 22 1478 6946 Fax +49 22 1478 6965 emailExpand
Cumulative inactivation of N-type CaV2.2 calcium channels modified by alternative splicing.
TLDR
Alternative splicing of an exon in a cytoplasmic region of the Ca(V)2.2 channel modulates its sensitivity to inactivation during trains of action potential waveforms, suggesting a possible mechanism for modulating short-term dynamics of synaptic efficacy in different regions of the nervous system. Expand
The cytosolic II–III loop of Cav2.3 provides an essential determinant for the phorbol ester‐mediated stimulation of E–type Ca2+ channel activity
TLDR
Receptor independent stimulation of PKC and its interaction with Cav2.3 channels represents an important positive feedback mechanism to decode electrical signals into a variety of cellular functions and is suggested to augmenting Ca2+ influx into the cytosol. Expand
Cav2.3 Ca2+ Channel Interacts with the G1-subunit of V-ATPase
TLDR
The results suggest that v-ATPase interacts physically and also functionally with Cav2.3, the first demonstration of association of Cav 2.3 C-terminus with a protein complex which is involved in transmembrane signalling. Expand
In vitro and in vivo phosphorylation of the Cav2.3 voltage-gated R-type calcium channel
TLDR
Findings indicate that ATP promotes phosphorylation of either the channel or an associated protein, whereas dephosphorylation during cell dialysis results in run-down. Expand
Cav2.3 R-type calcium channels: from its discovery to pathogenic de novo CACNA1E variants: a historical perspective
TLDR
So-called pharmacoresistant (R-type) voltage-gated Ca 2+ channels are structurally only partially characterized and easier activation by spontaneous mutations or lack of bioavailable inorganic cations may lead to similar pathologies caused by cellular overexcitation. Expand
the molecular chaperone hsp70
TLDR
The results suggest that the Ca v 2.3 interaction partner, Hsp70, and its membrane association are important for understanding the molecular events in kainate-induced hippocampal neurodegeneration. Expand
The neuronal splicing factor Nova controls alternative splicing in N-type and P-type CaV2 calcium channels
TLDR
It is likely that coordinated alternative pre-mRNA splicing across related CaV2 genes by common splicing factors, allows neurons to orchestrate changes in synaptic protein function while maintaining a balanced and functioning system. Expand
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