title: The Ca2+-induced methyltransferase xPRMT1b controls neural fate in amphibian embryo.
abstract: We have previously shown that an increase in intracellular Ca2+ is both necessary and sufficient to commit ectoderm to a neural fate in Xenopus embryos. However, the relationship between this Ca2+ increase and the expression of early neural genes has yet to be defined. Using a subtractive cDNA library between untreated and caffeine-treated animal caps, i.e., control ectoderm and ectoderm induced toward a neural fate by a release of Ca2+, we have isolated the arginine N-methyltransferase, xPRMT1b, a Ca2+-induced target gene, which plays a pivotal role in this process. First, we show in embryo and in animal cap that xPRMT1b expression is Ca2+-regulated. Second, overexpression of xPRMT1b induces the expression of early neural genes such as Zic3. Finally, in the whole embryo, antisense approach with morpholino oligonucleotide against xPRMT1b impairs neural development and in animal caps blocks the expression of neural markers induced by a release of internal Ca2+. Our results implicate an instructive role of an enzyme, an arginine methyltransferase protein, in the embryonic choice of determination between epidermal and neural fate. The results presented provide insights by which a Ca2+ increase induces neural fate.
authors.affiliation: Centre de Biologie du Développement, Groupment de Recherche 2688, Unite Mixte de Recherche 5547, Centre National de la Recherche Scientifique, 118 Route de Narbonne, 31062 Toulouse Cedex 04, France.
authors.forename: Julie
authors.initials: J
authors.lastname: Batut
authors.forename: Laurence
authors.initials: L
authors.lastname: Vandel
authors.forename: Catherine
authors.initials: C
authors.lastname: Leclerc
authors.forename: Christiane
authors.initials: C
authors.lastname: Daguzan
authors.forename: Marc
authors.initials: M
authors.lastname: Moreau
authors.forename: Isabelle
authors.initials: I
authors.lastname: Néant
mesh_terms: D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D002110:Caffeine / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D019070:Cell Lineage; D004625:Embryo, Nonmammalian / Q000187:drug effects / Q000201:enzymology*; D004628:Embryonic Structures / Q000166:cytology / Q000378:metabolism; D005775:Gastrula / Q000502:physiology; D018507:Gene Expression Regulation, Developmental; D017403:In Situ Hybridization; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009474:Neurons / Q000166:cytology / Q000502:physiology*; D016376:Oligonucleotides, Antisense / Q000235:genetics / Q000378:metabolism; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000196:embryology*; D000099176:Noggin Protein
chemical_list: D015415:Biomarkers; D002110:Caffeine; D002118:Calcium; D002352:Carrier Proteins; D007527:Isoenzymes; D008780:Methyltransferases; D016376:Oligonucleotides, Antisense; D011484:Protein-Arginine N-Methyltransferases; D029867:Xenopus Proteins; D000099176:Noggin Protein; C505834:PRMT1b protein, Xenopus