GlutaredoxinV1, Main, Exploration, bibRecord, 000535

Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity.

Identifieur interne : 000535 ( Main/Exploration ); précédent : 000534; suivant : 000536

Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity.

Auteurs : Heba Al Khamici [Australie] ; Louise J. Brown [Australie] ; Khondker R. Hossain [Australie] ; Amanda L. Hudson [Australie] ; Alxcia A. Sinclair-Burton [Australie] ; Jane Phui Mun Ng [Australie] ; Elizabeth L. Daniel [Australie] ; Joanna E. Hare [Australie] ; Bruce A. Cornell [Australie] ; Paul M G. Curmi [Australie] ; Mary W. Davey [Australie] ; Stella M. Valenzuela [Australie]

Source :

PloS one [ 1932-6203 ] ; 2015.

RBID : pubmed:25581026

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Chloride Channels (metabolism), Glutaredoxins (metabolism), Glutathione Transferase (metabolism), Models, Molecular (MeSH), Protein Conformation (MeSH), Protein Structure, Tertiary (MeSH).
MESH :
- chemical , metabolism : Chloride Channels, Glutaredoxins, Glutathione Transferase.
- Amino Acid Sequence, Models, Molecular, Protein Conformation, Protein Structure, Tertiary.

Abstract

The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins where they function as chloride selective ion channels, however no function has previously been assigned to their soluble form. Structural studies have shown that in the soluble form, CLIC proteins adopt a glutathione S-transferase (GST) fold, however, they have an active site with a conserved glutaredoxin monothiol motif, similar to the omega class GSTs. We demonstrate that CLIC proteins have glutaredoxin-like glutathione-dependent oxidoreductase enzymatic activity. CLICs 1, 2 and 4 demonstrate typical glutaredoxin-like activity using 2-hydroxyethyl disulfide as a substrate. Mutagenesis experiments identify cysteine 24 as the catalytic cysteine residue in CLIC1, which is consistent with its structure. CLIC1 was shown to reduce sodium selenite and dehydroascorbate in a glutathione-dependent manner. Previous electrophysiological studies have shown that the drugs IAA-94 and A9C specifically block CLIC channel activity. These same compounds inhibit CLIC1 oxidoreductase activity. This work for the first time assigns a functional activity to the soluble form of the CLIC proteins. Our results demonstrate that the soluble form of the CLIC proteins has an enzymatic activity that is distinct from the channel activity of their integral membrane form. This CLIC enzymatic activity may be important for protecting the intracellular environment against oxidation. It is also likely that this enzymatic activity regulates the CLIC ion channel function.

DOI: 10.1371/journal.pone.0115699
PubMed: 25581026
PubMed Central: PMC4291220

Affiliations:

Australie

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000564
to stream Main, to step Curation: 000564

Le document en format XML

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<term>Glutaredoxins (metabolism)</term>
<term>Glutathione Transferase (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Canaux chlorure (métabolisme)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathione transferase (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chloride Channels</term>
<term>Glutaredoxins</term>
<term>Glutathione Transferase</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Canaux chlorure</term>
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<term>Models, Molecular</term>
<term>Protein Conformation</term>
<term>Protein Structure, Tertiary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term>
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<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins where they function as chloride selective ion channels, however no function has previously been assigned to their soluble form. Structural studies have shown that in the soluble form, CLIC proteins adopt a glutathione S-transferase (GST) fold, however, they have an active site with a conserved glutaredoxin monothiol motif, similar to the omega class GSTs. We demonstrate that CLIC proteins have glutaredoxin-like glutathione-dependent oxidoreductase enzymatic activity. CLICs 1, 2 and 4 demonstrate typical glutaredoxin-like activity using 2-hydroxyethyl disulfide as a substrate. Mutagenesis experiments identify cysteine 24 as the catalytic cysteine residue in CLIC1, which is consistent with its structure. CLIC1 was shown to reduce sodium selenite and dehydroascorbate in a glutathione-dependent manner. Previous electrophysiological studies have shown that the drugs IAA-94 and A9C specifically block CLIC channel activity. These same compounds inhibit CLIC1 oxidoreductase activity. This work for the first time assigns a functional activity to the soluble form of the CLIC proteins. Our results demonstrate that the soluble form of the CLIC proteins has an enzymatic activity that is distinct from the channel activity of their integral membrane form. This CLIC enzymatic activity may be important for protecting the intracellular environment against oxidation. It is also likely that this enzymatic activity regulates the CLIC ion channel function. </div>
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<Month>12</Month>
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<Abstract><AbstractText>The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins where they function as chloride selective ion channels, however no function has previously been assigned to their soluble form. Structural studies have shown that in the soluble form, CLIC proteins adopt a glutathione S-transferase (GST) fold, however, they have an active site with a conserved glutaredoxin monothiol motif, similar to the omega class GSTs. We demonstrate that CLIC proteins have glutaredoxin-like glutathione-dependent oxidoreductase enzymatic activity. CLICs 1, 2 and 4 demonstrate typical glutaredoxin-like activity using 2-hydroxyethyl disulfide as a substrate. Mutagenesis experiments identify cysteine 24 as the catalytic cysteine residue in CLIC1, which is consistent with its structure. CLIC1 was shown to reduce sodium selenite and dehydroascorbate in a glutathione-dependent manner. Previous electrophysiological studies have shown that the drugs IAA-94 and A9C specifically block CLIC channel activity. These same compounds inhibit CLIC1 oxidoreductase activity. This work for the first time assigns a functional activity to the soluble form of the CLIC proteins. Our results demonstrate that the soluble form of the CLIC proteins has an enzymatic activity that is distinct from the channel activity of their integral membrane form. This CLIC enzymatic activity may be important for protecting the intracellular environment against oxidation. It is also likely that this enzymatic activity regulates the CLIC ion channel function. </AbstractText>
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<ForeName>Heba</ForeName>
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<ForeName>Louise J</ForeName>
<Initials>LJ</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry and Bimolecular Sciences, Macquarie University, Sydney, New South Wales 2109, Australia.</Affiliation>
</AffiliationInfo>
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<ForeName>Khondker R</ForeName>
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</AffiliationInfo>
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<Initials>EL</Initials>
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Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity.

Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity.

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