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  • 1.
    Berger, Birgit S.
    et al.
    Division of Molecular Embryology, DKFZ‐ZMBH Alliance, Heidelberg, Germany.
    Acebron, Sergio P.
    Division of Molecular Embryology, DKFZ‐ZMBH Alliance, Heidelberg, Germany.
    Herbst, Jessica
    Division of Molecular Embryology, DKFZ‐ZMBH Alliance, Heidelberg, Germany.
    Koch, Stefan
    Division of Molecular Embryology, DKFZ‐ZMBH Alliance, Heidelberg, Germany.
    Niehrs, Christof
    Division of Molecular Embryology, DKFZ‐ZMBH Alliance, Heidelberg, Germany; Institute of Molecular Biology, Mainz, Germany.
    Parkinson's disease-associated receptor GPR37 is an ER chaperone for LRP62017In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 18, no 5, p. 712-725Article in journal (Refereed)
    Abstract [en]

    Wnt/beta-catenin signaling plays a key role in embryonic development, stem cell biology, and neurogenesis. However, the mechanisms of Wnt signal transmission, notably how the receptors are regulated, remain incompletely understood. Here we describe that the Parkinson's disease-associated receptor GPR37 functions in the maturation of the N-terminal bulky beta-propellers of the Wnt co-receptor LRP6. GPR37 is required for Wnt/beta-catenin signaling and protects LRP6 from ER-associated degradation via CHIP (carboxyl terminus of Hsc70-interacting protein) and the ATPase VCP GPR37 is highly expressed in neural progenitor cells (NPCs) where it is required for Wnt-dependent neurogenesis. We conclude that GPR37 is crucial for cellular protein quality control during Wnt signaling.

  • 2.
    Cantù, Claudio
    et al.
    Institute of Molecular Life Sciences, University of Zurich, Switzerland.
    Valenta, Tomas
    Institute of Molecular Life Sciences, University of Zurich, Switzerland.
    Basler, Konrad
    Institute of Molecular Life Sciences, University of Zurich, Switzerland.
    A RING finger to wed TCF and β-catenin2013In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 14, no 4, p. 295-296Article in journal (Refereed)
  • 3.
    Heilbronner, Goetz
    et al.
    University of Tubingen, Germany .
    Eisele, Yvonne S.
    University of Tubingen, Germany .
    Langer, Franziska
    University of Tubingen, Germany .
    Kaeser, Stephan A.
    University of Tubingen, Germany .
    Novotny, Renata
    University of Tubingen, Germany .
    Nagarathinam, Amudha
    University of Tubingen, Germany .
    Åslund, Andreas
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Hammarström, Per
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Nilsson, Peter
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
    Jucker, Mathias
    University of Tubingen, Germany .
    Seeded strain-like transmission of beta-amyloid morphotypes in APP transgenic mice2013In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 14, no 11, p. 1017-1022Article in journal (Refereed)
    Abstract [en]

    The polymorphic beta-amyloid lesions present in individuals with Alzheimers disease are collectively known as cerebral beta-amyloidosis. Amyloid precursor protein (APP) transgenic mouse models similarly develop beta-amyloid depositions that differ in morphology, binding of amyloid conformation-sensitive dyes, and A beta 40/A beta 42 peptide ratio. To determine the nature of such beta-amyloid morphotypes, beta-amyloid-containing brain extracts from either aged APP23 brains or aged APPPS1 brains were intracerebrally injected into the hippocampus of young APP23 or APPPS1 transgenic mice. APPPS1 brain extract injected into young APP23 mice induced beta-amyloid deposition with the morphological, conformational, and A beta 40/A beta 42 ratio characteristics of beta-amyloid deposits in aged APPPS1 mice, whereas APP23 brain extract injected into young APP23 mice induced b-amyloid deposits with the characteristics of beta-amyloid deposits in aged APP23 mice. Injecting the two extracts into the APPPS1 host revealed a similar difference between the induced beta-amyloid deposits, although less prominent, and the induced deposits were similar to the beta-amyloid deposits found in aged APPPS1 hosts. These results indicate that the molecular composition and conformation of aggregated A beta in APP transgenic mice can be maintained by seeded conversion.

  • 4.
    Nava, Porfirio
    et al.
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Capaldo, Christopher T.
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Koch, Stefan
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Kolegraff, Keli
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Rankin, Carl Robert
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Farkas, Attila E.
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA; Institute of Biophysics, Biological Research Center, Szeged, Hungary.
    Feasel, Mattie E.
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Li, Linheng
    Stowers Institute for Medical Research, Kansas City, Missouri, USA.
    Addis, Caroline
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Parkos, Charles A.
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    Nusrat, Asma
    Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Whitehead Biomedical Research Building, Atlanta, Georgia, USA.
    JAM-A regulates epithelial proliferation through Akt/beta-catenin signalling2011In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 12, no 4, p. 314-20Article in journal (Refereed)
    Abstract [en]

    Expression of the tight junction protein junctional adhesion molecule-A (JAM-A) has been linked to proliferation and tumour progression. However, a direct role for JAM-A in regulating proliferative processes has not been shown. By using complementary in vivo and in vitro approaches, we demonstrate that JAM-A restricts intestinal epithelial cell (IEC) proliferation in a dimerization-dependent manner, by inhibiting Akt-dependent beta-catenin activation. Furthermore, IECs from transgenic JAM-A(-/-)/beta-catenin/T-cell factor reporter mice showed enhanced beta-catenin-dependent transcription. Finally, inhibition of Akt reversed colonic crypt hyperproliferation in JAM-A-deficient mice. These data establish a new link between JAM-A and IEC homeostasis.

  • 5. Vainio, Saara
    et al.
    Heino, Sanna
    Månsson, Jan-Eric
    Fredman, Pam
    Kuismanen, Esa
    Vaarala, Outi
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Molecular and Clinical Medicine, Pediatrics. Östergötlands Läns Landsting, Centre of Paediatrics and Gynecology and Obstetrics, Barn.
    Ikonen, Elina
    Dynamic association of human insulin receptor with lipid rafts in cells lacking caveolae.2002In: EMBO Reports, ISSN 1469-221X, E-ISSN 1469-3178, Vol. 3, p. 95-100Article in journal (Refereed)
1 - 5 of 5
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