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Analysis of Sp6 and Sp8 protein-protein interactions and DNA binding during limb development

AutorRos, María A. ; Pérez-Gómez, Rocío; Fernández-Guerrero, Marc; Zunzunegui, Sandra ; Bell, Sheila; López-Giménez, Juan F.
Fecha de publicación2017
CitaciónExperimental Biology Meeting (2017)
ResumenSp6 and Sp8, two members of the specificity protein (Sp) family of zinc-finger transcription factors, are expressed in the limb ectoderm. Their importance in limb development was demonstrated by the analysis of double null mutants that exhibited a range of limb malformations that correlated with the dose of Sp6/Sp8 gene products remained (Haro et al., 2014). Thus, the progressive reduction led to predictable morphologies that transit from syndactyly, to split-hand/foot malformation phenotype, oligodactyly, truncation and finally amelia. In addition, when digits form these show a double dorsal tip. The molecular study of these mutants revealed that Sp6 and Sp8 work together downstream to Wnt/bcatenin to activate Fgf8 and downstream of Bmp signaling, possible cooperating with Smads, to activate En1, the ventral determinant in limb patterning. Here, to further the understanding of Sp6/8 function, we have investigated Sp6/8 suspected protein-protein interactions by co-immunoprecipitation (CoIP) and by bimolecular fluorescence complementation (BiFC). To this end, Sp6, Sp8 and Smads were tagged with Myc or FLAG epitopes to their N-terminal end and with YFP full length or YFP moieties to their C-terminal end. Our results show that Sp6/8 form homo and heterodimers and that they form complexes with BMP R-Smads. All these interactions require the C-terminal domain of Sps. We are currently determining Sp6/8 DNA binding activity by luciferase reporter and EMSA assays.
DescripciónResumen del póster presentado al Experimental Biology Meeting, celebrado en Chicago (US) del 22 al 26 de abril de 2017.
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