The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle
The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle
Date
2016
Authors
Qadota, Hiroshi
Matsunaga, Yohei
McMurry, Jonathan L.
Wilson, Kristy J.
Kwon, Grace E.
Stanford, Rachel
Deehan, Kevin
Tinley, Tina L.
Benian, Guy M.
Editors
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
URI (citable link)
DOI (citable link)
International patent number
Link to the license
EU project number
Project
Open Access publication
Collections
Title in another language
Publication type
Journal article
Publication status
Published
Published in
Molecular Biology of the Cell ; 27 (2016), 10. - pp. 1606-1620. - ISSN 1044-2030. - eISSN 1939-4586
Abstract
UNC-89 is a giant polypeptide located at the sarcomeric M-line of Caenorhabditis elegans muscle. The human homologue is obscurin. To understand how UNC-89 is localized and functions, we have been identifying its binding partners. Screening a yeast two-hybrid library revealed that UNC-89 interacts with paramyosin. Paramyosin is an invertebrate-specific coiled-coil dimer protein that is homologous to the rod portion of myosin heavy chains and resides in thick filament cores. Minimally, this interaction requires UNC-89's SH3 domain and residues 294-376 of paramyosin and has a KD of ∼1.1 μM. In unc-89 loss-of-function mutants that lack the SH3 domain, paramyosin is found in accumulations. When the SH3 domain is overexpressed, paramyosin is mislocalized. SH3 domains usually interact with a proline-rich consensus sequence, but the region of paramyosin that interacts with UNC-89's SH3 is α-helical and lacks prolines. Homology modeling of UNC-89's SH3 suggests structural features that might be responsible for this interaction. The SH3-binding region of paramyosin contains a "skip residue," which is likely to locally unwind the coiled-coil and perhaps contributes to the binding specificity.
Summary in another language
Subject (DDC)
570 Biosciences, Biology
Keywords
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690
QADOTA, Hiroshi, Olga MAYANS, Yohei MATSUNAGA, Jonathan L. MCMURRY, Kristy J. WILSON, Grace E. KWON, Rachel STANFORD, Kevin DEEHAN, Tina L. TINLEY, Guy M. BENIAN, 2016. The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle. In: Molecular Biology of the Cell. 27(10), pp. 1606-1620. ISSN 1044-2030. eISSN 1939-4586. Available under: doi: 10.1091/mbc.E15-09-0675BibTex
@article{Qadota2016domai-34900, year={2016}, doi={10.1091/mbc.E15-09-0675}, title={The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle}, number={10}, volume={27}, issn={1044-2030}, journal={Molecular Biology of the Cell}, pages={1606--1620}, author={Qadota, Hiroshi and Mayans, Olga and Matsunaga, Yohei and McMurry, Jonathan L. and Wilson, Kristy J. and Kwon, Grace E. and Stanford, Rachel and Deehan, Kevin and Tinley, Tina L. and Benian, Guy M.} }
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/123456789/34900"> <dc:creator>Deehan, Kevin</dc:creator> <dcterms:title>The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle</dcterms:title> <dc:contributor>Mayans, Olga</dc:contributor> <dcterms:abstract xml:lang="eng">UNC-89 is a giant polypeptide located at the sarcomeric M-line of Caenorhabditis elegans muscle. The human homologue is obscurin. To understand how UNC-89 is localized and functions, we have been identifying its binding partners. Screening a yeast two-hybrid library revealed that UNC-89 interacts with paramyosin. Paramyosin is an invertebrate-specific coiled-coil dimer protein that is homologous to the rod portion of myosin heavy chains and resides in thick filament cores. Minimally, this interaction requires UNC-89's SH3 domain and residues 294-376 of paramyosin and has a KD of ∼1.1 μM. In unc-89 loss-of-function mutants that lack the SH3 domain, paramyosin is found in accumulations. When the SH3 domain is overexpressed, paramyosin is mislocalized. SH3 domains usually interact with a proline-rich consensus sequence, but the region of paramyosin that interacts with UNC-89's SH3 is α-helical and lacks prolines. Homology modeling of UNC-89's SH3 suggests structural features that might be responsible for this interaction. The SH3-binding region of paramyosin contains a "skip residue," which is likely to locally unwind the coiled-coil and perhaps contributes to the binding specificity.</dcterms:abstract> <dc:language>eng</dc:language> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/34900/1/Qadota_0-343414.pdf"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Qadota, Hiroshi</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/34900"/> <dc:creator>Stanford, Rachel</dc:creator> <dc:rights>terms-of-use</dc:rights> <dc:contributor>Stanford, Rachel</dc:contributor> <dc:creator>Wilson, Kristy J.</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-07-28T12:36:50Z</dc:date> <dc:contributor>Deehan, Kevin</dc:contributor> <dc:creator>McMurry, Jonathan L.</dc:creator> <dc:contributor>Wilson, Kristy J.</dc:contributor> <dc:creator>Kwon, Grace E.</dc:creator> <dc:creator>Mayans, Olga</dc:creator> <dc:contributor>Tinley, Tina L.</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-07-28T12:36:50Z</dcterms:available> <dc:contributor>Benian, Guy M.</dc:contributor> <dc:contributor>Qadota, Hiroshi</dc:contributor> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Benian, Guy M.</dc:creator> <dc:contributor>Matsunaga, Yohei</dc:contributor> <dc:contributor>McMurry, Jonathan L.</dc:contributor> <dc:creator>Matsunaga, Yohei</dc:creator> <dcterms:issued>2016</dcterms:issued> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/34900/1/Qadota_0-343414.pdf"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:contributor>Kwon, Grace E.</dc:contributor> <dc:creator>Tinley, Tina L.</dc:creator> </rdf:Description> </rdf:RDF>
Internal note
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Examination date of dissertation
Method of financing
Comment on publication
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
Yes