Twitchin kinase inhibits muscle activity

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MATSUNAGA, Yohei, Hyundoo HWANG, Barbara FRANKE, Rhys WILLIAMS, McKenna PENLEY, Hiroshi QADOTA, Hong YI, Levi T. MORRAN, Hang LU, Olga MAYANS, Guy M. BENIAN, 2017. Twitchin kinase inhibits muscle activity. In: Molecular Biology of the Cell. 28(12), pp. 1591-1600. ISSN 1059-1524. eISSN 1939-4586

@article{Matsunaga2017-06-15Twitc-39598, title={Twitchin kinase inhibits muscle activity}, year={2017}, doi={10.1091/mbc.E16-10-0707}, number={12}, volume={28}, issn={1059-1524}, journal={Molecular Biology of the Cell}, pages={1591--1600}, author={Matsunaga, Yohei and Hwang, Hyundoo and Franke, Barbara and Williams, Rhys and Penley, McKenna and Qadota, Hiroshi and Yi, Hong and Morran, Levi T. and Lu, Hang and Mayans, Olga and Benian, Guy M.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/39598"> <dc:creator>Benian, Guy M.</dc:creator> <dc:contributor>Qadota, Hiroshi</dc:contributor> <dc:creator>Lu, Hang</dc:creator> <dcterms:issued>2017-06-15</dcterms:issued> <dcterms:abstract xml:lang="eng">Muscle sarcomeres contain giant polypeptides composed of multiple immunoglobulin and fibronectin domains and one or two protein kinase domains. Although binding partners for a number of this family's kinase domains have been identified, the catalytic necessity of these kinase domains remains unknown. In addition, various members of this kinase family are suspected pseudokinases with no or little activity. Here we address catalytic necessity for the first time, using the prototypic invertebrate representative twitchin (UNC-22) from Caenorhabditis elegans In in vitro experiments, change of a conserved lysine (K) that is involved in ATP coordination to alanine (A) resulted in elimination of kinase activity without affecting the overall structure of the kinase domain. The same mutation, unc-22(sf21), was generated in the endogenous twitchin gene. The unc-22(sf21) worms have well-organized sarcomeres. However, unc-22(sf21) mutants move faster than wild-type worms and, by optogenetic experiments, contract more. Wild-type nematodes exhibited greater competitive fitness than unc-22(sf21) mutants. Thus the catalytic activity of twitchin kinase has a role in vivo, where it inhibits muscle activity and is likely maintained by selection.</dcterms:abstract> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-07-18T09:07:51Z</dc:date> <dc:creator>Yi, Hong</dc:creator> <dc:contributor>Penley, McKenna</dc:contributor> <dc:creator>Williams, Rhys</dc:creator> <dc:language>eng</dc:language> <dc:creator>Qadota, Hiroshi</dc:creator> <dc:creator>Matsunaga, Yohei</dc:creator> <dc:contributor>Matsunaga, Yohei</dc:contributor> <dc:contributor>Morran, Levi T.</dc:contributor> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/39598"/> <dc:creator>Morran, Levi T.</dc:creator> <dc:creator>Hwang, Hyundoo</dc:creator> <dc:contributor>Franke, Barbara</dc:contributor> <dc:contributor>Lu, Hang</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-07-18T09:07:51Z</dcterms:available> <dc:contributor>Mayans, Olga</dc:contributor> <dc:contributor>Hwang, Hyundoo</dc:contributor> <dc:creator>Penley, McKenna</dc:creator> <dc:contributor>Yi, Hong</dc:contributor> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150914100631302-4485392-8"/> <dc:creator>Franke, Barbara</dc:creator> <dc:contributor>Williams, Rhys</dc:contributor> <dcterms:title>Twitchin kinase inhibits muscle activity</dcterms:title> <dc:contributor>Benian, Guy M.</dc:contributor> <dc:creator>Mayans, Olga</dc:creator> </rdf:Description> </rdf:RDF>

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