GlutaredoxinV1, Main, Exploration, bibRecord, 000702

The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.

Identifieur interne : 000702 ( Main/Exploration ); précédent : 000701; suivant : 000703

The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.

Auteurs : Marcus Cebula [Suède] ; Naazneen Moolla ; Alexio Capovilla ; Elias S J. Arnér

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2013.

RBID : pubmed:23413027

Descripteurs français

English descriptors

KwdEn :
- Acylation (MeSH), Alternative Splicing (MeSH), Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Catalytic Domain (MeSH), Cell Line, Tumor (MeSH), Cysteine (genetics), Glutaredoxins (chemistry), Green Fluorescent Proteins (metabolism), HEK293 Cells (MeSH), Humans (MeSH), Lipids (chemistry), Membrane Microdomains (metabolism), Molecular Sequence Data (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Protein Structure, Tertiary (MeSH), Pseudopodia (metabolism), Recombinant Fusion Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Signal Transduction (MeSH), Thioredoxin Reductase 1 (chemistry), Thioredoxin Reductase 1 (genetics).
MESH :
- chemical , chemistry : Glutaredoxins, Lipids, Thioredoxin Reductase 1.
- chemical , genetics : Cysteine, Thioredoxin Reductase 1.
- chemical , metabolism : Green Fluorescent Proteins, Recombinant Fusion Proteins.
- metabolism : Membrane Microdomains, Pseudopodia.
- Acylation, Alternative Splicing, Amino Acid Motifs, Amino Acid Sequence, Catalytic Domain, Cell Line, Tumor, HEK293 Cells, Humans, Molecular Sequence Data, Mutation, Oxidation-Reduction, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Signal Transduction.

Abstract

The human selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene, is a key player in redox regulation. Alternative splicing generates several TrxR1 variants, one of which is v3 that carries an atypical N-terminal glutaredoxin domain. When overexpressed, v3 associates with membranes and triggers formation of filopodia. Here we found that membrane targeting of v3 is mediated by myristoylation and palmitoylation of its N-terminal MGC motif, through which v3 specifically targets membrane rafts. This was suggested by its localization in cholera toxin subunit B-stained membrane areas and also shown using lipid fractionation experiments. Utilizing site-directed mutant variants, we also found that v3-mediated generation of filopodia is independent of the Cys residues in its redox active site, but dependent upon its membrane raft targeting. These results identify v3 as an intricately regulated protein that expands TXNRD1-derived protein functions to the membrane raft compartment.

DOI: 10.1074/jbc.M112.445932
PubMed: 23413027
PubMed Central: PMC3617239

Affiliations:

Suède

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

to stream Main, to step Corpus: 000762
to stream Main, to step Curation: 000762

Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
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<term>Cysteine (genetics)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Green Fluorescent Proteins (metabolism)</term>
<term>HEK293 Cells (MeSH)</term>
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<term>Recombinant Fusion Proteins (metabolism)</term>
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<term>Cellules HEK293 (MeSH)</term>
<term>Cystéine (génétique)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Humains (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Lipides (composition chimique)</term>
<term>Microdomaines membranaires (métabolisme)</term>
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<term>Oxydoréduction (MeSH)</term>
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<term>Protéines à fluorescence verte (métabolisme)</term>
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<term>Séquence d'acides aminés (MeSH)</term>
<term>Thioredoxin reductase 1 (composition chimique)</term>
<term>Thioredoxin reductase 1 (génétique)</term>
<term>Transduction du signal (MeSH)</term>
<term>Épissage alternatif (MeSH)</term>
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<term>Thioredoxin Reductase 1</term>
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<term>Thioredoxin reductase 1</term>
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<term>Thioredoxin reductase 1</term>
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<term>Pseudopodia</term>
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<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Mutation</term>
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<term>Protein Structure, Tertiary</term>
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<term>Données de séquences moléculaires</term>
<term>Humains</term>
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<term>Mutation</term>
<term>Oxydoréduction</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The human selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene, is a key player in redox regulation. Alternative splicing generates several TrxR1 variants, one of which is v3 that carries an atypical N-terminal glutaredoxin domain. When overexpressed, v3 associates with membranes and triggers formation of filopodia. Here we found that membrane targeting of v3 is mediated by myristoylation and palmitoylation of its N-terminal MGC motif, through which v3 specifically targets membrane rafts. This was suggested by its localization in cholera toxin subunit B-stained membrane areas and also shown using lipid fractionation experiments. Utilizing site-directed mutant variants, we also found that v3-mediated generation of filopodia is independent of the Cys residues in its redox active site, but dependent upon its membrane raft targeting. These results identify v3 as an intricately regulated protein that expands TXNRD1-derived protein functions to the membrane raft compartment.</div>
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<ArticleTitle>The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.</ArticleTitle>
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<Abstract><AbstractText>The human selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene, is a key player in redox regulation. Alternative splicing generates several TrxR1 variants, one of which is v3 that carries an atypical N-terminal glutaredoxin domain. When overexpressed, v3 associates with membranes and triggers formation of filopodia. Here we found that membrane targeting of v3 is mediated by myristoylation and palmitoylation of its N-terminal MGC motif, through which v3 specifically targets membrane rafts. This was suggested by its localization in cholera toxin subunit B-stained membrane areas and also shown using lipid fractionation experiments. Utilizing site-directed mutant variants, we also found that v3-mediated generation of filopodia is independent of the Cys residues in its redox active site, but dependent upon its membrane raft targeting. These results identify v3 as an intricately regulated protein that expands TXNRD1-derived protein functions to the membrane raft compartment.</AbstractText>
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   |texte=   The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.
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The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.

The rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.

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