title: Domain analysis of the Nematostella vectensis SNAIL ortholog reveals unique nucleolar localization that depends on the zinc-finger domains.
abstract: SNAIL transcriptional factors are key regulators during development and disease. They arose early during evolution, and in cnidarians such as Nematostella vectensis, NvSNAILA/B are detected in invaginating tissues during gastrulation. The function of SNAIL proteins is well established in bilaterians but their roles in cnidarians remain unknown. The structure of NvSNAILA and B is similar to the human SNAIL1 and 2, including SNAG and zinc-finger domains. Here, we performed a molecular analysis on localization and mobility of NvSNAILA/B using mammalian cells and Nematostella embryos. NvSNAILA/B display nuclear localization and mobility similar to HsSNAIL1/2. Strikingly, NvSNAILA is highly enriched in the nucleoli and shuttles between the nucleoli and the nucleoplasm. Truncation of the N-terminal SNAG domain, reported to contain Nuclear Localization Signals, markedly reduces nucleolar levels, without effecting nuclear localization or mobility. Truncation of the C-terminal zinc-fingers, involved in DNA binding in higher organisms, significantly affects subcellular localization and mobility. Specifically, the zinc-finger domains are required for nucleolar enrichment of NvSNAILA. Differently from SNAIL transcriptional factors described before, NvSNAILA is specifically enriched in the nucleoli co-localizing with nucleolar markers even after nucleolar disruption. Our findings implicate additional roles for SNAG and zinc-finger domains, suggesting a role for NvSNAILA in the nucleolus.
authors.affiliation: Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam Science Park 904, NL-1098 XH Amsterdam The Netherlands.
authors.forename: Ada A
authors.initials: AA
authors.lastname: Dattoli
authors.affiliation: 1] Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam Science Park 904, NL-1098 XH Amsterdam The Netherlands [2] van Leeuwenhoek Centre for Advanced Microscopy (LCAM), University of Amsterdam, Science Park 904, NL-1098 XH Amsterdam The Netherlands.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Hink
authors.affiliation: The Whitney Laboratory for Marine Bioscience 9505 Ocean Shore Blvd, St. Augustine, FL 32080-8610.
authors.forename: Timothy Q
authors.initials: TQ
authors.lastname: DuBuc
authors.affiliation: Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam Science Park 904, NL-1098 XH Amsterdam The Netherlands.
authors.forename: Bram J
authors.initials: BJ
authors.lastname: Teunisse
authors.affiliation: Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam Science Park 904, NL-1098 XH Amsterdam The Netherlands.
authors.forename: Joachim
authors.initials: J
authors.lastname: Goedhart
authors.affiliation: 1] Université Nice Sophia Antipolis, IRCAN, UMR 7284, 06107 Nice, France [2] CNRS, IRCAN, UMR 7284, 06107 Nice, France [3] INSERM, IRCAN, U1081, 06107 Nice, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Röttinger
authors.affiliation: Molecular Cytology, Swammerdam Institute for Life Sciences, University of Amsterdam Science Park 904, NL-1098 XH Amsterdam The Netherlands.
authors.forename: Marten
authors.initials: M
authors.lastname: Postma
mesh_terms: D021581:Active Transport, Cell Nucleus; D000595:Amino Acid Sequence; D000818:Animals; D002466:Cell Nucleolus / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D042541:Intracellular Space; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D009154:Mutation; D019913:Nuclear Localization Signals; D010802:Phylogeny; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D012615:Sea Anemones / Q000378:metabolism*; D016415:Sequence Alignment; D000071250:Snail Family Transcription Factors; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016335:Zinc Fingers
chemical_list: D019913:Nuclear Localization Signals; C000604407:SNAI1 protein, human; D000071250:Snail Family Transcription Factors; D014157:Transcription Factors; D003546:Cysteine Endopeptidases