A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.
Identifieur interne : 000684 ( PubMed/Curation ); précédent : 000683; suivant : 000685A 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.
Descripteurs français
- KwdFr :
- Animaux, Calcium (métabolisme), Calcium (pharmacologie), Calmoduline (métabolisme), Canaux potassiques éther-à-go-go (), Canaux potassiques éther-à-go-go (métabolisme), Dipeptides (pharmacologie), Données de séquences moléculaires, Espace intracellulaire (métabolisme), Humains, Lignée cellulaire, Modèles biologiques, Motifs d'acides aminés, Mutation (génétique), Mâle, Ouverture et fermeture des portes des canaux ioniques (), Protéines mutantes (), Protéines mutantes (métabolisme), Protéolyse (), Rat Sprague-Dawley, Séquence d'acides aminés, Taille de la cellule ().
- MESH :
- génétique : Mutation.
- métabolisme : Calcium, Calmoduline, Canaux potassiques éther-à-go-go, Espace intracellulaire, Protéines mutantes.
- pharmacologie : Calcium, Dipeptides.
- Animaux, Canaux potassiques éther-à-go-go, Données de séquences moléculaires, Humains, Lignée cellulaire, Modèles biologiques, Motifs d'acides aminés, Mâle, Ouverture et fermeture des portes des canaux ioniques, Protéines mutantes, Protéolyse, Rat Sprague-Dawley, Séquence d'acides aminés, Taille de la cellule.
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
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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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25542181</PMID><DateCreated><Year>2015</Year><Month>01</Month><Day>19</Day></DateCreated><DateCompleted><Year>2015</Year><Month>09</Month><Day>18</Day></DateCompleted><DateRevised><Year>2015</Year><Month>01</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-5875</ISSN><JournalIssue CitedMedium="Internet"><Volume>59</Volume><PubDate><Year>2015</Year><Month>Feb</Month></PubDate></JournalIssue><Title>The international journal of biochemistry & cell biology</Title><ISOAbbreviation>Int. J. Biochem. Cell Biol.</ISOAbbreviation></Journal><ArticleTitle>A sustained increase in the intracellular Ca²⁺ concentration induces proteolytic cleavage of EAG2 channel.</ArticleTitle><Pagination><MedlinePgn>126-34</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.biocel.2014.12.007</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1357-2725(14)00399-9</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shimizu</LastName><ForeName>Nobuhiro</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Natsumi</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kikuchi</LastName><ForeName>Teppei</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ishizaki</LastName><ForeName>Takuro</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kobayashi</LastName><ForeName>Kazuto</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kita</LastName><ForeName>Kaori</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA 15261, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takimoto</LastName><ForeName>Koichi</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan; Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA 15261, United States. Electronic address: koichi@vos.nagaokaut.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>12</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biochem Cell Biol</MedlineTA><NlmUniqueID>9508482</NlmUniqueID><ISSNLinking>1357-2725</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002147">Calmodulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004151">Dipeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051638">Ether-A-Go-Go Potassium Channels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C485729">KCNH5 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>88191-84-8</RegistryNumber><NameOfSubstance UI="C058076">calpain inhibitor III</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" 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PubStatus="revised"><Year>2014</Year><Month>11</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>12</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>12</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>12</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25542181</ArticleId><ArticleId IdType="pii">S1357-2725(14)00399-9</ArticleId><ArticleId IdType="doi">10.1016/j.biocel.2014.12.007</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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