NF2/Merlin is required for the axial pattern formation in the Xenopus laevis embryo

Mechanisms of Development
Xuechen ZhuQinghua Tao

Abstract

The NF2 gene product Merlin is a FERM-domain protein possessing a broad tumor-suppressing function. NF2/Merlin has been implicated in regulating multiple signaling pathways critical for cell growth and survival. However, it remains unknown whether NF2/Merlin regulates Wnt/β-catenin signaling during vertebrate embryogenesis. Here we demonstrate that NF2/Merlin is required for body pattern formation in the Xenopus laevis embryo. Depletion of the maternal NF2/Merlin enhances organizer gene expression dependent on the presence of β-catenin, and causes dorsanteriorized development; Morpholino antisense oligo-mediated knockdown of the zygotic NF2/Merlin shifts posterior genes anteriorwards and reduces the anterior development. We further demonstrate that targeted depletion of NF2 in the presumptive dorsal tissues increases the levels of nuclear β-catenin in the neural epithelial cells. Biochemical analyses reveal that NF2 depletion promotes the production of active β-catenin and concurrently decreases the level of N-terminally phosphorylated β-catenin under the stimulation of the endogenous Wnt signaling. Our findings suggest that NF2/Merlin negatively regulates the Wnt/β-catenin signaling activity during the pattern formation in ear...Continue Reading

References

Jan 1, 1994·Human Molecular Genetics·E C TwistG A Rouleau
Apr 2, 2003·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Pascal PineauAnne Dejean
Apr 16, 2003·Genes & Development·Dominique LallemandAndrea I McClatchey
Mar 6, 2004·Science·W James Nelson, Roel Nusse
Sep 9, 2006·Science·Tobias SjöblomVictor E Velculescu
Mar 16, 2007·Proceedings of the National Academy of Sciences of the United States of America·Margaret E McLaughlinTyler Jacks
Sep 9, 2009·Development·Renée van Amerongen, Roel Nusse
Dec 17, 2009·Cell·Christian P Petersen, Peter W Reddien
Jan 5, 2010·Methods : a Companion to Methods in Enzymology·Alissa M HulstrandDouglas W Houston
Aug 3, 2010·Genes & Development·Samira BenhamoucheAndrea I McClatchey
Jun 12, 2012·Cell·Hans Clevers, Roel Nusse
Aug 23, 2012·PloS One·Lucas B MurrayQin Yu
Oct 23, 2012·Cold Spring Harbor Perspectives in Biology·Cristina-Maria Cruciat, Christof Niehrs
Nov 10, 2012·Science·Ana R HernándezMarc W Kirschner
Jun 25, 2013·Current Biology : CB·Katie CockburnJanet Rossant
Apr 15, 2014·FEBS Letters·Jonathan Cooper, Filippo G Giancotti

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Citations

Oct 30, 2016·Acta Biochimica Et Biophysica Sinica·Zheying MinQinghua Tao
Apr 15, 2019·Experimental Eye Research·Surabhi SonamJonathan J Henry
Feb 24, 2021·Development, Growth & Differentiation·Gabriele Colozza, Bon-Kyoung Koo

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