Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/108555
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKorrodi-Gregório, Luís-
dc.contributor.authorLopes, Ana Margarida-
dc.contributor.authorEsteves, Sara L. C.-
dc.contributor.authorAfonso, Sandra-
dc.contributor.authorLemos de Matos, Ana-
dc.contributor.authorLissovsky, Andrey A.-
dc.contributor.authorCruz e Silva, Odete A. B. da-
dc.contributor.authorCruz e Silva, Edgar F. da-
dc.contributor.authorEsteves, Pedro José-
dc.contributor.authorFardilha, Margarida-
dc.date.accessioned2017-03-17T11:24:19Z-
dc.date.available2017-03-17T11:24:19Z-
dc.date.issued2013-10-10-
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/2445/108555-
dc.description.abstractT-complex testis expressed protein 1 domain containing 4 (TCTEX1D4) contains the canonical phosphoprotein phosphatase 1 (PPP1) binding motif, composed by the amino acid sequence RVSF. We identified and validated the binding of TCTEX1D4 to PPP1 and demonstrated that indeed this protein is a novel PPP1 interacting protein. Analyses of twenty-one mammalian species available in public databases and seven Lagomorpha sequences obtained in this work showed that the PPP1 binding motif 90RVSF93 is present in all of them and is flanked by a palindromic sequence, PLGS, except in three species of pikas (Ochotona princeps, O. dauurica and O. pusilla). Furthermore, for the Ochotona species an extra glycosylation site, motif 96NLS98, and the loss of the palindromic sequence were observed. Comparison with other lagomorphs suggests that this event happened before the Ochotona radiation. The dN/dS for the sequence region comprising the PPP1 binding motif and the flanking palindrome highly supports the hypothesis that for Ochotona species this region has been evolving under positive selection. In addition, mutational screening shows that the ability of pikas TCTEX1D4 to bind to PPP1 is maintained, although the PPP1 binding motif is disrupted, and the N- and C-terminal surrounding residues are also abrogated. These observations suggest pika as an ideal model to study novel PPP1 complexes regulatory mechanisms.-
dc.format.extent11 p.-
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherPublic Library of Science (PLoS)-
dc.relation.isformatofReproducció del document publicat a: https://doi.org/10.1371/journal.pone.007723-
dc.relation.ispartofPLoS One, 2013, vol. 8, num. 10, p. e77236-
dc.relation.urihttps://doi.org/10.1371/journal.pone.007723-
dc.rightscc-by (c) Korrodi-Gregório, Luís et al., 2013-
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es-
dc.sourceArticles publicats en revistes (Patologia i Terapèutica Experimental)-
dc.subject.classificationMutagènesi-
dc.subject.classificationSelecció natural-
dc.subject.classificationLagomorfs-
dc.subject.classificationFosfatases-
dc.subject.otherMutagenesis-
dc.subject.otherNatural selection-
dc.subject.otherLagomorpha-
dc.subject.otherPhosphatases-
dc.titleAn intriguing shift occurs in the novel protein phosphatase 1 binding partner, TCTEX1D4: evidence of positive selection in a pika model-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.identifier.idgrec665650-
dc.date.updated2017-03-17T11:24:19Z-
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess-
dc.identifier.pmid24130861-
Appears in Collections:Articles publicats en revistes (Patologia i Terapèutica Experimental)

Files in This Item:
File Description SizeFormat 
665650.pdf3.85 MBAdobe PDFView/Open


This item is licensed under a Creative Commons License Creative Commons