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Molecular basis of AKAP79 regulation by calmodulin

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PATEL, Neha, Florian STENGEL, Ruedi AEBERSOLD, Matthew GOLD, 2017. Molecular basis of AKAP79 regulation by calmodulin. In: Nature communications. 8(1), 1681. eISSN 2041-1723. Available under: doi: 10.1038/s41467-017-01715-w

@article{Patel2017-11-22Molec-40961, title={Molecular basis of AKAP79 regulation by calmodulin}, year={2017}, doi={10.1038/s41467-017-01715-w}, 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 xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:issued>2017-11-22</dcterms:issued> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:isPartOf rdf:resource=""/> <dspace:hasBitstream rdf:resource=""/> <dc:creator>Aebersold, Ruedi</dc:creator> <dc:language>eng</dc:language> <dcterms:rights rdf:resource=""/> <dcterms:hasPart rdf:resource=""/> <dcterms:available rdf:datatype="">2017-12-19T13:05:02Z</dcterms:available> <dc:creator>Patel, Neha</dc:creator> <dc:creator>Gold, Matthew</dc:creator> <dc:contributor>Stengel, Florian</dc:contributor> <dc:date rdf:datatype="">2017-12-19T13:05:02Z</dc:date> <bibo:uri rdf:resource=""/> <dc:contributor>Patel, Neha</dc:contributor> <dc:rights>Attribution 4.0 International</dc:rights> <dc:contributor>Aebersold, Ruedi</dc:contributor> <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> <dc:creator>Stengel, Florian</dc:creator> <dc:contributor>Gold, Matthew</dc:contributor> <dcterms:title>Molecular basis of AKAP79 regulation by calmodulin</dcterms:title> </rdf:Description> </rdf:RDF>

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