Christophe Royer
Wellcome Trust Postdoctoral Research Assistant
Christophe received his Bachelor of Science degree from the University of Strasbourg, France in 2002 and was awarded a Maters Degree in Molecular Pharmacology the following year. He earned a PhD from University College London in 2008 after investigating the cross-talks between Wnt signalling and the tumour supressor ASPP2. He moved to the University of Oxford with the Ludwig Institute for Cancer Research to pursue postdoctoral studies, investigating the role of apicobasal polarity during central nervous system development. In 2013, he joined the laboratory of Shankar Srinivas as a James Martin Stem Cell Research Fellow. His research interests now lie in understanding the mechanistic role of cellular architecture in directing cell fate decisions during early embryonic development.
Key publications
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ASPP2 links the apical lateral polarity complex to the regulation of YAP activity in epithelial cells.
Journal article
Royer C. et al, (2014), PLoS One, 9
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ASPP2 binds Par-3 and controls the polarity and proliferation of neural progenitors during CNS development.
Journal article
Sottocornola R. et al, (2010), Dev Cell, 19, 126 - 137
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Epithelial cell polarity: a major gatekeeper against cancer?
Journal article
Royer C. and Lu X., (2011), Cell Death Differ, 18, 1470 - 1477
Recent publications
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Mechanics of mouse blastocyst hatching revealed by a hydrogel-based microdeformation assay.
Journal article
Leonavicius K. et al, (2018), Proc Natl Acad Sci U S A, 115, 10375 - 10380
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Towards understanding the roles of position and geometry on cell fate decisions during preimplantation development.
Journal article
Biggins JS. et al, (2015), Semin Cell Dev Biol, 47-48, 74 - 79
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ASPP2 controls epithelial plasticity and inhibits metastasis through β-catenin-dependent regulation of ZEB1.
Journal article
Wang Y. et al, (2014), Nat Cell Biol, 16, 1092 - 1104
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ASPP2 links the apical lateral polarity complex to the regulation of YAP activity in epithelial cells.
Journal article
Royer C. et al, (2014), PLoS One, 9
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Inhibitory member of the apoptosis-stimulating proteins of the p53 family (iASPP) interacts with protein phosphatase 1 via a noncanonical binding motif.
Journal article
Llanos S. et al, (2011), J Biol Chem, 286, 43039 - 43044