Adaptive protein divergence of BMP ligands takes place under developmental and evolutionary constraints

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dc.contributor.author Tauscher, Petra
dc.contributor.author Gui, Jinghua
dc.contributor.author Shimmi, Osamu
dc.date.accessioned 2017-02-08T15:01:01Z
dc.date.available 2017-02-08T15:01:01Z
dc.date.issued 2016-10-18
dc.identifier.citation Tauscher , P , Gui , J & Shimmi , O 2016 , ' Adaptive protein divergence of BMP ligands takes place under developmental and evolutionary constraints ' , Development , vol. 143 , no. 20 , pp. 3742-3750 . https://doi.org/10.1242/dev.130427
dc.identifier.other PURE: 77148486
dc.identifier.other PURE UUID: b3b648ad-7cbd-46e1-9e46-93664cefcd6d
dc.identifier.other Scopus: 84991777375
dc.identifier.other WOS: 000393452500010
dc.identifier.other ORCID: /0000-0001-6341-9130/work/30224281
dc.identifier.other ORCID: /0000-0003-2474-500X/work/35988437
dc.identifier.other ORCID: /0000-0003-4452-1716/work/30226046
dc.identifier.uri http://hdl.handle.net/10138/174903
dc.description.abstract The bone morphogenetic protein (BMP) signaling network, comprising evolutionary conserved BMP2/4/Decapentaplegic (Dpp) and Chordin/Short gastrulation (Sog), is widely utilized for dorsal-ventral (DV) patterning during animal development. A similar network is required for posterior crossvein (PCV) formation in the Drosophila pupal wing. Although both transcriptional and post-transcriptional regulation of co-factors in the network gives rise to tissue-specific and species-specific properties, their mechanisms are incompletely understood. In Drosophila, BMP5/6/7/8-type ligands, Screw (Scw) and Glass bottom boat (Gbb), form heterodimers with Dpp for DV patterning and PCV development, respectively. Sequence analysis indicates that the Scw ligand contains two N-glycosylation motifs: one being highly conserved between BMP2/4- and BMP5/6/7/8-type ligands, and the other being Scw ligand specific. Our data reveal that N-glycosylation of the Scw ligand boosts BMP signaling both in cell culture and in the embryo. In contrast, N-glycosylation modifications of Gbb or Scw ligands reduce the consistency of PCV development. These results suggest that tolerance for structural changes of BMP5/6/7/8-type ligands is dependent on developmental constraints. Furthermore, gain and loss of N-glycosylation motifs in conserved signaling molecules under evolutionary constraints appear to constitute flexible modules to adapt to developmental processes. en
dc.format.extent 9
dc.language.iso eng
dc.relation.ispartof Development
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject 1184 Genetics, developmental biology, physiology
dc.subject Drosophila melanogaster
dc.subject PROTEIN EVOLUTION
dc.subject 1182 Biochemistry, cell and molecular biology
dc.subject Glycosylation
dc.title Adaptive protein divergence of BMP ligands takes place under developmental and evolutionary constraints en
dc.type Article
dc.contributor.organization Institute of Biotechnology
dc.contributor.organization Morphogenesis and cellular dynamics
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1242/dev.130427
dc.relation.issn 0950-1991
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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