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Characterization of the first honeybee Ca2+ channel subunit reveals two novel species- and splicing-specific modes of regulation of channel inactivation

Overview of attention for article published in Pflugers Archiv European Journal of Physiology, April 2013
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Title
Characterization of the first honeybee Ca2+ channel subunit reveals two novel species- and splicing-specific modes of regulation of channel inactivation
Published in
Pflugers Archiv European Journal of Physiology, April 2013
DOI 10.1007/s00424-013-1223-2
Pubmed ID
Authors

Thierry Cens, Matthieu Rousset, Claude Collet, Valérie Raymond, Fabien Démares, Annabelle Quintavalle, Michel Bellis, Yves Le Conte, Mohamed Chahine, Pierre Charnet

Abstract

The honeybee is a model system to study learning and memory, and Ca(2+) signals play a key role in these processes. We have cloned, expressed, and characterized the first honeybee Ca(2+) channel subunit. We identified two splice variants of the Apis CaVβ Ca(2+) channel subunit (Am-CaVβ) and demonstrated expression in muscle and neurons. Although AmCaVβ shares with vertebrate CaVβ subunits the SH3 and GK domains, it beholds a unique N terminus that is alternatively spliced in the first exon to produce a long (a) and short (b) variant. When expressed with the CaV2 channels both, AmCaVβa and AmCaVβb, increase current amplitude, shift the voltage-sensitivity of the channel, and slow channel inactivation as the vertebrate CaVβ2a subunit does. However, as opposed to CaVβ2a, slow inactivation induced by Am-CaVβa was insensitive to palmitoylation but displayed a unique PI3K sensitivity. Inactivation produced by the b variant was PI3K-insensitive but staurosporine/H89-sensitive. Deletion of the first exon suppressed the sensitivity to PI3K inhibitors, staurosporine, or H89. Recording of Ba(2+) currents in Apis neurons or muscle cells evidenced a sensitivity to PI3K inhibitors and H89, suggesting that both AmCaVβ variants may be important to couple cell signaling to Ca(2+) entry in vivo. Functional interactions with phospho-inositide and identification of phosphorylation sites in AmCaVβa and AmCaVβb N termini, respectively, suggest that AmCaVβ splicing promoted two novel and alternative modes of regulation of channel activity with specific signaling pathways. This is the first description of a splicing-dependent kinase switch in the regulation of Ca(2+) channel activity by CaVβ subunit.

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Mendeley readers

The data shown below were compiled from readership statistics for 25 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Germany 1 4%
United Kingdom 1 4%
Unknown 23 92%

Demographic breakdown

Readers by professional status Count As %
Researcher 10 40%
Unspecified 4 16%
Professor 3 12%
Student > Master 3 12%
Student > Ph. D. Student 2 8%
Other 3 12%
Readers by discipline Count As %
Agricultural and Biological Sciences 15 60%
Unspecified 5 20%
Neuroscience 2 8%
Biochemistry, Genetics and Molecular Biology 1 4%
Environmental Science 1 4%
Other 1 4%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 August 2013.
All research outputs
#9,764,365
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Outputs from Pflugers Archiv European Journal of Physiology
#985
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Outputs of similar age
#101,245
of 148,918 outputs
Outputs of similar age from Pflugers Archiv European Journal of Physiology
#8
of 15 outputs
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