title: Zic1 controls placode progenitor formation non-cell autonomously by regulating retinoic acid production and transport.
abstract: All cranial placode progenitors arise from a common precursor field anterior to the neural plate, the pre-placodal region (PPR). We showed that transcription factor Zic1, expressed at the anterior neural plate, is necessary and sufficient to promote placode fate. Here we reveal the non-cell autonomous activity of Zic1 and implicate retinoic acid (RA) signalling as a key player in cranial placode progenitor specification. In a screen for genes activated by Zic1, we identify several factors involved in RA metabolism and function. Among them we show that retinaldehyde dehydrogenase 2 (RALDH2) and lipocalin-type prostaglandin D2 synthase (LPGDS), which, respectively, regulate the synthesis and transport of RA, directly participate in the establishment of the PPR. We propose that RALDH2 and LPGDS induction by Zic1 at the anterior neural plate allows for the localized production and transport of RA, which in turn activates a cranial placode developmental programme in neighbouring cells.
authors.affiliation: Department of Basic Science and Craniofacial Biology, New York University, College of Dentistry, 345 East 24th street, New York, New York 10010, USA.
authors.forename: Maria Belen
authors.initials: MB
authors.lastname: Jaurena
authors.affiliation: Department of Basic Science and Craniofacial Biology, New York University, College of Dentistry, 345 East 24th street, New York, New York 10010, USA.
authors.forename: Hugo
authors.initials: H
authors.lastname: Juraver-Geslin
authors.affiliation: Department of Basic Science and Craniofacial Biology, New York University, College of Dentistry, 345 East 24th street, New York, New York 10010, USA.
authors.forename: Arun
authors.initials: A
authors.lastname: Devotta
authors.affiliation: Department of Basic Science and Craniofacial Biology, New York University, College of Dentistry, 345 East 24th street, New York, New York 10010, USA.
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Saint-Jeannet
mesh_terms: D000080924:Aldehyde Dehydrogenase 1 Family; D042931:Aldehyde Oxidase / Q000235:genetics / Q000378:metabolism; D000818:Animals; D004475:Ectoderm / Q000196:embryology* / Q000378:metabolism; D004625:Embryo, Nonmammalian; D018507:Gene Expression Regulation, Developmental; D017403:In Situ Hybridization; D019746:Intramolecular Oxidoreductases / Q000235:genetics / Q000378:metabolism; D054834:Lipocalins / Q000235:genetics / Q000378:metabolism; D054258:Neural Plate / Q000196:embryology / Q000378:metabolism; D055495:Neurogenesis / Q000235:genetics*; D012333:RNA, Messenger / Q000378:metabolism*; D060888:Real-Time Polymerase Chain Reaction; D050697:Retinal Dehydrogenase; D015398:Signal Transduction; D013234:Stem Cells / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism; D014212:Tretinoin / Q000378:metabolism*; D029867:Xenopus Proteins / Q000235:genetics* / Q000378:metabolism; D014982:Xenopus laevis
chemical_list: D054834:Lipocalins; D012333:RNA, Messenger; D014157:Transcription Factors; D029867:Xenopus Proteins; C116546:Zic1 protein, Xenopus; D014212:Tretinoin; D000080924:Aldehyde Dehydrogenase 1 Family; D050697:Retinal Dehydrogenase; C493756:aldh1a2 protein, Xenopus; D042931:Aldehyde Oxidase; D019746:Intramolecular Oxidoreductases; C022466:prostaglandin R2 D-isomerase