CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex

Zhou, Tiankun; Fleming, Jennifer R.; Franke, Barbara; Bogomolovas, Julius; Barsukov, Igor; Rigden, Daniel J.; Labeit, Siegfried; Mayans, Olga

CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex

Dateien

Zhou_0-383148.pdfGröße: 2.21 MBDownloads: 599

Datum

2016

Autor:innen

Zhou, Tiankun

Fleming, Jennifer R.

Franke, Barbara

Bogomolovas, Julius

Barsukov, Igor

Rigden, Daniel J.

Labeit, Siegfried

Mayans, Olga

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

FEBS Letters. 2016, 590(18), pp. 3098-3110. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1002/1873-3468.12362

Zusammenfassung

The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated α-helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

ZHOU, Tiankun, Jennifer R. FLEMING, Barbara FRANKE, Julius BOGOMOLOVAS, Igor BARSUKOV, Daniel J. RIGDEN, Siegfried LABEIT, Olga MAYANS, 2016. CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex. In: FEBS Letters. 2016, 590(18), pp. 3098-3110. ISSN 0014-5793. eISSN 1873-3468. Available under: doi: 10.1002/1873-3468.12362

BibTex

@article{Zhou2016-09inter-36547,
  year={2016},
  doi={10.1002/1873-3468.12362},
  title={CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex},
  number={18},
  volume={590},
  issn={0014-5793},
  journal={FEBS Letters},
  pages={3098--3110},
  author={Zhou, Tiankun and Fleming, Jennifer R. and Franke, Barbara and Bogomolovas, Julius and Barsukov, Igor and Rigden, Daniel J. and Labeit, Siegfried and Mayans, Olga}
}

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/123456789/36547">
    <dc:contributor>Bogomolovas, Julius</dc:contributor>
    <dc:language>eng</dc:language>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Fleming, Jennifer R.</dc:contributor>
    <dc:contributor>Labeit, Siegfried</dc:contributor>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/36547/1/Zhou_0-383148.pdf"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/36547/1/Zhou_0-383148.pdf"/>
    <dc:creator>Zhou, Tiankun</dc:creator>
    <dcterms:abstract xml:lang="eng">The cardiac ankyrin repeat protein (CARP) is up-regulated in the myocardium during cardiovascular disease and in response to mechanical or toxic stress. Stress-induced CARP interacts with the N2A spring region of the titin filament to modulate muscle compliance. We characterize the interaction between CARP and titin-N2A and show that the binding site in titin spans the dual domain UN2A-Ig81. We find that the unique sequence UN2A is not structurally disordered, but that it has a stable, elongated α-helical fold that possibly acts as a constant force spring. Our findings portray CARP/titin-N2A as a structured node and help to rationalize the molecular basis of CARP mechanosensing in the sarcomeric I-band.</dcterms:abstract>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Mayans, Olga</dc:contributor>
    <dc:creator>Barsukov, Igor</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Labeit, Siegfried</dc:creator>
    <dc:creator>Mayans, Olga</dc:creator>
    <dc:creator>Fleming, Jennifer R.</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-01-10T13:22:33Z</dcterms:available>
    <dc:contributor>Zhou, Tiankun</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-01-10T13:22:33Z</dc:date>
    <dc:rights>terms-of-use</dc:rights>
    <dcterms:title>CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex</dcterms:title>
    <dc:contributor>Barsukov, Igor</dc:contributor>
    <dc:creator>Bogomolovas, Julius</dc:creator>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/36547"/>
    <dc:contributor>Franke, Barbara</dc:contributor>
    <dcterms:issued>2016-09</dcterms:issued>
    <dc:contributor>Rigden, Daniel J.</dc:contributor>
    <dc:creator>Rigden, Daniel J.</dc:creator>
    <dc:creator>Franke, Barbara</dc:creator>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja