Role of Interaction and Nucleoside Diphosphate Kinase B in Regulation of the Cystic Fibrosis Transmembrane Conductance Regulator Function by cAMP-Dependent Protein Kinase A
Identifieur interne : 000061 ( France/Analysis ); précédent : 000060; suivant : 000062Role of Interaction and Nucleoside Diphosphate Kinase B in Regulation of the Cystic Fibrosis Transmembrane Conductance Regulator Function by cAMP-Dependent Protein Kinase A
Auteurs : Lee A. Borthwick [Royaume-Uni] ; Mathieu Kerbiriou [Royaume-Uni] ; Christopher J. Taylor [Royaume-Uni] ; Giorgio Cozza [Italie] ; Ioan Lascu [France] ; Edith H. Postel [États-Unis] ; Diane Cassidy [Royaume-Uni] ; Pascal Trouvé [France] ; Anil Mehta [Royaume-Uni] ; Louise Robson [Royaume-Uni] ; Richmond Muimo [Royaume-Uni]Source :
- PLoS ONE [ 1932-6203 ] ; 2016.
Descripteurs français
- KwdFr :
- AMP cyclique (métabolisme), Animaux, Appareil respiratoire (cytologie), Cellules épithéliales (cytologie), Cyclic AMP-Dependent Protein Kinases (métabolisme), Cytosol (métabolisme), Données de séquences moléculaires, Humains, Jeune adulte, Liaison aux protéines, Lignée cellulaire, Membrane cellulaire (métabolisme), Modèles moléculaires, NM23 Nucleoside Diphosphate kinases (), NM23 Nucleoside Diphosphate kinases (métabolisme), Polarité de la cellule, Protéine CFTR (), Protéine CFTR (métabolisme), Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Transport de protéines.
- MESH :
- cytologie : Appareil respiratoire, Cellules épithéliales.
- métabolisme : AMP cyclique, Cyclic AMP-Dependent Protein Kinases, Cytosol, Membrane cellulaire, NM23 Nucleoside Diphosphate kinases, Protéine CFTR.
- Animaux, Données de séquences moléculaires, Humains, Jeune adulte, Liaison aux protéines, Lignée cellulaire, Modèles moléculaires, NM23 Nucleoside Diphosphate kinases, Polarité de la cellule, Protéine CFTR, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés, Transport de protéines.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cell Membrane (metabolism), Cell Polarity, Cyclic AMP (metabolism), Cyclic AMP-Dependent Protein Kinases (metabolism), Cystic Fibrosis Transmembrane Conductance Regulator (chemistry), Cystic Fibrosis Transmembrane Conductance Regulator (metabolism), Cytosol (metabolism), Epithelial Cells (cytology), Humans, Models, Molecular, Molecular Sequence Data, NM23 Nucleoside Diphosphate Kinases (chemistry), NM23 Nucleoside Diphosphate Kinases (metabolism), Protein Binding, Protein Structure, Tertiary, Protein Transport, Respiratory System (cytology), Young Adult.
- MESH :
- chemical , chemistry : Cystic Fibrosis Transmembrane Conductance Regulator, NM23 Nucleoside Diphosphate Kinases.
- chemical , metabolism : Cyclic AMP, Cyclic AMP-Dependent Protein Kinases, Cystic Fibrosis Transmembrane Conductance Regulator, NM23 Nucleoside Diphosphate Kinases.
- cytology : Epithelial Cells, Respiratory System.
- metabolism : Cell Membrane, Cytosol.
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cell Polarity, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Protein Transport, Young Adult.
Abstract
Cystic fibrosis results from mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), a cAMP-dependent protein kinase A (PKA) and ATP-regulated chloride channel. Here, we demonstrate that nucleoside diphosphate kinase B (NDPK-B, NM23-H2) forms a functional complex with CFTR. In airway epithelia forskolin/IBMX significantly increases NDPK-B co-localisation with CFTR whereas PKA inhibitors attenuate complex formation. Furthermore, an NDPK-B derived peptide (but not its NDPK-A equivalent) disrupts the NDPK-B/CFTR complex
Url:
DOI: 10.1371/journal.pone.0149097
PubMed: 26950439
PubMed Central: 4780765
Affiliations:
- France, Italie, Royaume-Uni, États-Unis
- Aquitaine, New Jersey, Nouvelle-Aquitaine, Région Bretagne
- Bordeaux, Brest
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PMC:4780765Le document en format XML
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</nlm:aff>
<country xml:lang="fr">France</country>
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<author><name sortKey="Cassidy, Diane" sort="Cassidy, Diane" uniqKey="Cassidy D" first="Diane" last="Cassidy">Diane Cassidy</name>
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</nlm:aff>
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</nlm:aff>
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</nlm:aff>
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<author><name sortKey="Muimo, Richmond" sort="Muimo, Richmond" uniqKey="Muimo R" first="Richmond" last="Muimo">Richmond Muimo</name>
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</nlm:aff>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Binding Sites</term>
<term>Cell Line</term>
<term>Cell Membrane (metabolism)</term>
<term>Cell Polarity</term>
<term>Cyclic AMP (metabolism)</term>
<term>Cyclic AMP-Dependent Protein Kinases (metabolism)</term>
<term>Cystic Fibrosis Transmembrane Conductance Regulator (chemistry)</term>
<term>Cystic Fibrosis Transmembrane Conductance Regulator (metabolism)</term>
<term>Cytosol (metabolism)</term>
<term>Epithelial Cells (cytology)</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>NM23 Nucleoside Diphosphate Kinases (chemistry)</term>
<term>NM23 Nucleoside Diphosphate Kinases (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Transport</term>
<term>Respiratory System (cytology)</term>
<term>Young Adult</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>AMP cyclique (métabolisme)</term>
<term>Animaux</term>
<term>Appareil respiratoire (cytologie)</term>
<term>Cellules épithéliales (cytologie)</term>
<term>Cyclic AMP-Dependent Protein Kinases (métabolisme)</term>
<term>Cytosol (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Jeune adulte</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Modèles moléculaires</term>
<term>NM23 Nucleoside Diphosphate kinases ()</term>
<term>NM23 Nucleoside Diphosphate kinases (métabolisme)</term>
<term>Polarité de la cellule</term>
<term>Protéine CFTR ()</term>
<term>Protéine CFTR (métabolisme)</term>
<term>Sites de fixation</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Transport de protéines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cystic Fibrosis Transmembrane Conductance Regulator</term>
<term>NM23 Nucleoside Diphosphate Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cyclic AMP</term>
<term>Cyclic AMP-Dependent Protein Kinases</term>
<term>Cystic Fibrosis Transmembrane Conductance Regulator</term>
<term>NM23 Nucleoside Diphosphate Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Appareil respiratoire</term>
<term>Cellules épithéliales</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Epithelial Cells</term>
<term>Respiratory System</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Cytosol</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>AMP cyclique</term>
<term>Cyclic AMP-Dependent Protein Kinases</term>
<term>Cytosol</term>
<term>Membrane cellulaire</term>
<term>NM23 Nucleoside Diphosphate kinases</term>
<term>Protéine CFTR</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Binding Sites</term>
<term>Cell Line</term>
<term>Cell Polarity</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Transport</term>
<term>Young Adult</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Jeune adulte</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Modèles moléculaires</term>
<term>NM23 Nucleoside Diphosphate kinases</term>
<term>Polarité de la cellule</term>
<term>Protéine CFTR</term>
<term>Sites de fixation</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Transport de protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Cystic fibrosis results from mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), a cAMP-dependent protein kinase A (PKA) and ATP-regulated chloride channel. Here, we demonstrate that nucleoside diphosphate kinase B (NDPK-B, NM23-H2) forms a functional complex with CFTR. In airway epithelia forskolin/IBMX significantly increases NDPK-B co-localisation with CFTR whereas PKA inhibitors attenuate complex formation. Furthermore, an NDPK-B derived peptide (but not its NDPK-A equivalent) disrupts the NDPK-B/CFTR complex <italic>in vitro</italic>
(19-mers comprising amino acids 36–54 from NDPK-B or NDPK-A). Overlay (Far-Western) and Surface Plasmon Resonance (SPR) analysis both demonstrate that NDPK-B binds CFTR within its first nucleotide binding domain (NBD1, CFTR amino acids 351–727). Analysis of chloride currents reflective of CFTR or outwardly rectifying chloride channels (ORCC, DIDS-sensitive) showed that the 19-mer NDPK-B peptide (but not its NDPK-A equivalent) reduced both chloride conductances. Additionally, the NDPK-B (but not NDPK-A) peptide also attenuated acetylcholine-induced intestinal short circuit currents. <italic>In silico</italic>
analysis of the NBD1/NDPK-B complex reveals an extended interaction surface between the two proteins. This binding zone is also target of the 19-mer NDPK-B peptide, thus confirming its capability to disrupt NDPK-B/CFTR complex. We propose that NDPK-B forms part of the complex that controls chloride currents in epithelia.</p>
</div>
</front>
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<name sortKey="Taylor, Christopher J" sort="Taylor, Christopher J" uniqKey="Taylor C" first="Christopher J." last="Taylor">Christopher J. Taylor</name>
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<country name="Italie"><noRegion><name sortKey="Cozza, Giorgio" sort="Cozza, Giorgio" uniqKey="Cozza G" first="Giorgio" last="Cozza">Giorgio Cozza</name>
</noRegion>
</country>
<country name="France"><region name="Nouvelle-Aquitaine"><name sortKey="Lascu, Ioan" sort="Lascu, Ioan" uniqKey="Lascu I" first="Ioan" last="Lascu">Ioan Lascu</name>
</region>
<name sortKey="Trouve, Pascal" sort="Trouve, Pascal" uniqKey="Trouve P" first="Pascal" last="Trouvé">Pascal Trouvé</name>
</country>
<country name="États-Unis"><region name="New Jersey"><name sortKey="Postel, Edith H" sort="Postel, Edith H" uniqKey="Postel E" first="Edith H." last="Postel">Edith H. Postel</name>
</region>
</country>
</tree>
</affiliations>
</record>
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