PittsburghV1, Main, Exploration, bibRecord, 000648

A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.

Identifieur interne : 000648 ( Main/Exploration ); précédent : 000647; suivant : 000649

A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.

Auteurs : Nobuhiro Shimizu [Japon] ; Natsumi Sato [Japon] ; Teppei Kikuchi [Japon] ; Takuro Ishizaki [Japon] ; Kazuto Kobayashi [Japon] ; Kaori Kita [États-Unis] ; Koichi Takimoto [États-Unis]

Source :

The international journal of biochemistry & cell biology [ 1878-5875 ] ; 2015.

RBID : pubmed:25542181

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Animals, Calcium (metabolism), Calcium (pharmacology), Calmodulin (metabolism), Cell Line, Cell Size (drug effects), Dipeptides (pharmacology), Ether-A-Go-Go Potassium Channels (chemistry), Ether-A-Go-Go Potassium Channels (metabolism), Humans, Intracellular Space (metabolism), Ion Channel Gating (drug effects), Male, Models, Biological, Molecular Sequence Data, Mutant Proteins (chemistry), Mutant Proteins (metabolism), Mutation (genetics), Proteolysis (drug effects), Rats, Sprague-Dawley.
MESH :
- chemical , chemistry : Ether-A-Go-Go Potassium Channels, Mutant Proteins.
- chemical , metabolism : Calcium, Calmodulin, Ether-A-Go-Go Potassium Channels, Mutant Proteins.
- chemical , pharmacology : Calcium, Dipeptides.
- drug effects : Cell Size, Ion Channel Gating, Proteolysis.
- genetics : Mutation.
- metabolism : Intracellular Space.
- Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, Humans, Male, Models, Biological, Molecular Sequence Data, Rats, Sprague-Dawley.

Abstract

Voltage-gated EAG2 channel is abundant in the brain and enhances cancer cell growth by controlling cell volume. The channel contains a cyclic nucleotide-binding homology (CNBH) domain and multiple calmodulin-binding motifs. Here we show that a raised intracellular Ca(2+) concentration causes proteolytic digestion of heterologously expressed and native EAG2 channels. A treatment of EAG2-expressing cells with the Ca(2+) ionophore A23187 for 1h reduces the full-length protein by ∼80% with a concomitant appearance of 30-35-kDa peptides. Similarly, a treatment with the Ca(2+)-ATPase inhibitor thapsigargin for 3h removes 30-35-kDa peptides from ∼1/3 of the channel protein. Moreover, an incubation of the isolated rat brain membrane with CaCl2 leads to the generation of fragments with similar sizes. This Ca(2+)-induced digestion is not seen with EAG1. Mutations in a C-terminal calmodulin-binding motif alter the degrees and positions of the cleavage. Truncated channels that mimic the digested proteins exhibit a reduced current density and altered channel gating. In particular, these shorter channels lack a rapid activation typical in EAG channels with more than 20-mV positive shifts in voltage dependence of activation. The truncation also eliminates the ability of EAG2 channel to reduce cell volume. These results suggest that a sustained increase in the intracellular Ca(2+) concentration leads to proteolytic cleavage at the C-terminal cytosolic region following the CNBH domain by altering its interaction with calmodulin. The observed Ca(2+)-induced proteolytic cleavage of EAG2 channel may act as an adaptive response under physiological and/or pathological conditions.

DOI: 10.1016/j.biocel.2014.12.007
PubMed: 25542181

Affiliations:

Le document en format XML

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<term>Calcium (pharmacology)</term>
<term>Calmodulin (metabolism)</term>
<term>Cell Line</term>
<term>Cell Size (drug effects)</term>
<term>Dipeptides (pharmacology)</term>
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<term>Calcium (métabolisme)</term>
<term>Calcium (pharmacologie)</term>
<term>Calmoduline (métabolisme)</term>
<term>Canaux potassiques éther-à-go-go ()</term>
<term>Canaux potassiques éther-à-go-go (métabolisme)</term>
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<term>Données de séquences moléculaires</term>
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<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Modèles biologiques</term>
<term>Motifs d'acides aminés</term>
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<term>Mâle</term>
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<term>Dipeptides</term>
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<term>Ion Channel Gating</term>
<term>Proteolysis</term>
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<term>Lignée cellulaire</term>
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<term>Mâle</term>
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<front><div type="abstract" xml:lang="en">Voltage-gated EAG2 channel is abundant in the brain and enhances cancer cell growth by controlling cell volume. The channel contains a cyclic nucleotide-binding homology (CNBH) domain and multiple calmodulin-binding motifs. Here we show that a raised intracellular Ca(2+) concentration causes proteolytic digestion of heterologously expressed and native EAG2 channels. A treatment of EAG2-expressing cells with the Ca(2+) ionophore A23187 for 1h reduces the full-length protein by ∼80% with a concomitant appearance of 30-35-kDa peptides. Similarly, a treatment with the Ca(2+)-ATPase inhibitor thapsigargin for 3h removes 30-35-kDa peptides from ∼1/3 of the channel protein. Moreover, an incubation of the isolated rat brain membrane with CaCl2 leads to the generation of fragments with similar sizes. This Ca(2+)-induced digestion is not seen with EAG1. Mutations in a C-terminal calmodulin-binding motif alter the degrees and positions of the cleavage. Truncated channels that mimic the digested proteins exhibit a reduced current density and altered channel gating. In particular, these shorter channels lack a rapid activation typical in EAG channels with more than 20-mV positive shifts in voltage dependence of activation. The truncation also eliminates the ability of EAG2 channel to reduce cell volume. These results suggest that a sustained increase in the intracellular Ca(2+) concentration leads to proteolytic cleavage at the C-terminal cytosolic region following the CNBH domain by altering its interaction with calmodulin. The observed Ca(2+)-induced proteolytic cleavage of EAG2 channel may act as an adaptive response under physiological and/or pathological conditions.</div>
</front>
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A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.

A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.

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