Publikation: Molecular basis of AKAP79 regulation by calmodulin
Lade...
Dateien
Datum
2017
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Gold
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Nature communications. 2017, 8(1), 1681. eISSN 2041-1723. Available under: doi: 10.1038/s41467-017-01715-w
Zusammenfassung
AKAP79/150 is essential for coordinating second messenger-responsive enzymes in processes including synaptic long-term depression. Ca2+ directly regulates AKAP79 through its effector calmodulin (CaM), but the molecular basis of this regulation was previously unknown. Here, we report that CaM recognizes a '1-4-7-8' pattern of hydrophobic amino acids starting at Trp79 in AKAP79. Cross-linking coupled to mass spectrometry assisted mapping of the interaction site. Removal of the CaM-binding sequence in AKAP79 prevents formation of a Ca2+-sensitive interface between AKAP79 and calcineurin, and increases resting cellular PKA phosphorylation. We determined a crystal structure of CaM bound to a peptide encompassing its binding site in AKAP79. CaM adopts a highly compact conformation in which its open Ca2+-activated C-lobe and closed N-lobe cooperate to recognize a mixed α/310 helix in AKAP79. The structure guided a bioinformatic screen to identify potential sites in other proteins that may employ similar motifs for interaction with CaM.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Proteomics, X-ray crystallography
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690
PATEL, Neha, Florian STENGEL, Ruedi AEBERSOLD, Matthew GOLD, 2017. Molecular basis of AKAP79 regulation by calmodulin. In: Nature communications. 2017, 8(1), 1681. eISSN 2041-1723. Available under: doi: 10.1038/s41467-017-01715-wBibTex
@article{Patel2017-11-22Molec-40961,
year={2017},
doi={10.1038/s41467-017-01715-w},
title={Molecular basis of AKAP79 regulation by calmodulin},
number={1},
volume={8},
journal={Nature communications},
author={Patel, Neha and Stengel, Florian and Aebersold, Ruedi and Gold, Matthew},
note={Article Number: 1681}
}RDF
<rdf:RDF
xmlns:dcterms="http://purl.org/dc/terms/"
xmlns:dc="http://purl.org/dc/elements/1.1/"
xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
xmlns:bibo="http://purl.org/ontology/bibo/"
xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
xmlns:foaf="http://xmlns.com/foaf/0.1/"
xmlns:void="http://rdfs.org/ns/void#"
xmlns:xsd="http://www.w3.org/2001/XMLSchema#" >
<rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/40961">
<dc:rights>Attribution 4.0 International</dc:rights>
<dc:language>eng</dc:language>
<dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-12-19T13:05:02Z</dc:date>
<dcterms:issued>2017-11-22</dcterms:issued>
<dc:contributor>Stengel, Florian</dc:contributor>
<dc:creator>Aebersold, Ruedi</dc:creator>
<dc:creator>Patel, Neha</dc:creator>
<foaf:homepage rdf:resource="http://localhost:8080/"/>
<dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/40961"/>
<dcterms:abstract xml:lang="eng">AKAP79/150 is essential for coordinating second messenger-responsive enzymes in processes including synaptic long-term depression. Ca2+ directly regulates AKAP79 through its effector calmodulin (CaM), but the molecular basis of this regulation was previously unknown. Here, we report that CaM recognizes a '1-4-7-8' pattern of hydrophobic amino acids starting at Trp79 in AKAP79. Cross-linking coupled to mass spectrometry assisted mapping of the interaction site. Removal of the CaM-binding sequence in AKAP79 prevents formation of a Ca2+-sensitive interface between AKAP79 and calcineurin, and increases resting cellular PKA phosphorylation. We determined a crystal structure of CaM bound to a peptide encompassing its binding site in AKAP79. CaM adopts a highly compact conformation in which its open Ca2+-activated C-lobe and closed N-lobe cooperate to recognize a mixed α/310 helix in AKAP79. The structure guided a bioinformatic screen to identify potential sites in other proteins that may employ similar motifs for interaction with CaM.</dcterms:abstract>
<dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40961/1/Patel_2-1ua7g14yq6ibq5.pdf"/>
<dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-12-19T13:05:02Z</dcterms:available>
<dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40961/1/Patel_2-1ua7g14yq6ibq5.pdf"/>
<dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dcterms:rights rdf:resource="http://creativecommons.org/licenses/by/4.0/"/>
<dc:contributor>Patel, Neha</dc:contributor>
<dc:creator>Gold, Matthew</dc:creator>
<dc:creator>Stengel, Florian</dc:creator>
<dc:contributor>Aebersold, Ruedi</dc:contributor>
<dcterms:title>Molecular basis of AKAP79 regulation by calmodulin</dcterms:title>
<void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
<dc:contributor>Gold, Matthew</dc:contributor>
</rdf:Description>
</rdf:RDF>Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
