Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans

ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.

Detalhes bibliográficos
Autores: Schultheiss, Kira P., Craddock, Barbara P., Suga, Hiroshi, Miller, W. Todd
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/115597
Acesso em linha:http://hdl.handle.net/10261/115597
Access Level:acceso abierto
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spelling Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibransSchultheiss, Kira P.Craddock, Barbara P.Suga, HiroshiMiller, W. ToddACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.The development of the phosphotyrosine-based signaling system predated the evolution of multicellular animals. Single-celled choanoflagellates, the closest living relatives to metazoans, possess numerous tyrosine kinases, including Src family nonreceptor tyrosine kinases. Choanoflagellates also have Csk (C-terminal Src kinase), the enzyme that regulates Src in metazoans; however, choanoflagellate Csk kinases fail to repress the cognate Src. Here, we have cloned and characterized Src and Csk kinases from Ministeria vibrans, a filasterean (the sister group to metazoans and choanoflagellates). The two Src kinases (MvSrc1 and MvSrc2) are enzymatically active Src kinases, although they have low activity toward mammalian cellular proteins. Unexpectedly, MvSrc2 has significant Ser/Thr kinase activity. The Csk homologue (MvCsk) is enzymatically inactive and fails to repress MvSrc activity. We suggest that the low activity of MvCsk is due to sequences in the SH2-kinase interface, and we show that a point mutation in this region partially restores MvCsk activity. The inactivity of filasterean Csk kinases is consistent with a model in which the stringent regulation of Src family kinases arose more recently in evolution, after the split between choanoflagellates and multicellular animals. © 2014 American Chemical Society.Peer ReviewedAmerican Chemical SocietyConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2015201520142015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/115597reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1021/bi4016499Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1155972026-05-22T06:33:51Z
dc.title.none.fl_str_mv Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
title Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
spellingShingle Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
Schultheiss, Kira P.
title_short Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
title_full Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
title_fullStr Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
title_full_unstemmed Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
title_sort Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans
dc.creator.none.fl_str_mv Schultheiss, Kira P.
Craddock, Barbara P.
Suga, Hiroshi
Miller, W. Todd
author Schultheiss, Kira P.
author_facet Schultheiss, Kira P.
Craddock, Barbara P.
Suga, Hiroshi
Miller, W. Todd
author_role author
author2 Craddock, Barbara P.
Suga, Hiroshi
Miller, W. Todd
author2_role author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
publishDate 2014
dc.date.none.fl_str_mv 2014
2015
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/115597
url http://hdl.handle.net/10261/115597
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1021/bi4016499
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812429

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