title: EphrinB2 affects apical constriction in Xenopus embryos and is regulated by ADAM10 and flotillin-1.
abstract: The Eph/ephrin signalling pathways have a critical function in cell adhesion and repulsion, and thus play key roles in various morphogenetic events during development. Here we show that a decrease in ephrinB2 protein causes neural tube closure defects during Xenopus laevis embryogenesis. Such a decrease in ephrinB2 protein levels is observed on the loss of flotillin-1 scaffold protein, a newly identified ephrinB2-binding partner. This dramatic decline in ephrinB2 protein levels on the absence of flotillin-1 expression is specific, and is partly the result of an increased susceptibility to cleavage by the metalloprotease ADAM10. These findings indicate that flotillin-1 regulates ephrinB2 protein levels through ADAM10, and is required for appropriate neural tube morphogenesis in the Xenopus embryo.
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Yon Ju
authors.initials: YJ
authors.lastname: Ji
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Yoo-Seok
authors.initials: YS
authors.lastname: Hwang
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Kathleen
authors.initials: K
authors.lastname: Mood
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Hee-Jun
authors.initials: HJ
authors.lastname: Cho
authors.affiliation: ABRC, CMRI, School of Life Sciences, College of Natural Sciences, Kyungpook National University, Daegu 702-701, South Korea.
authors.forename: Hyun-Shik
authors.initials: HS
authors.lastname: Lee
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Emily
authors.initials: E
authors.lastname: Winterbottom
authors.affiliation: Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, Massachusetts 01003, USA.
authors.forename: Hélène
authors.initials: H
authors.lastname: Cousin
authors.affiliation: Laboratory of Cell and Developmental Signaling, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
authors.forename: Ira O
authors.initials: IO
authors.lastname: Daar
mesh_terms: D051722:ADAM Proteins / Q000378:metabolism*; D000818:Animals; D015153:Blotting, Western; D004625:Embryo, Nonmammalian / Q000502:physiology; D036388:Ephrin-B2 / Q000378:metabolism*; D047468:Immunoprecipitation; D008565:Membrane Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D009024:Morphogenesis / Q000502:physiology*; D009436:Neural Tube Defects / Q000196:embryology* / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D014982:Xenopus laevis / Q000196:embryology* / Q000378:metabolism
chemical_list: D036388:Ephrin-B2; D008565:Membrane Proteins; C106354:flotillins; D051722:ADAM Proteins