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  • 1
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    Requirement of prorenin receptor and vacuolar H+-ATPase-mediated acidification for Wnt signaling (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-01-23
    Description: Wnt/beta-catenin signaling is important in stem cell biology, embryonic development, and disease, including cancer. However, the mechanism of Wnt signal transmission, notably how the receptors are activated, remains incompletely understood. We found that the prorenin receptor (PRR) is a component of the Wnt receptor complex. PRR functions in a renin-independent manner as an adaptor between Wnt receptors and the vacuolar H+-adenosine triphosphatase (V-ATPase) complex. Moreover, PRR and V-ATPase were required to mediate Wnt signaling during antero-posterior patterning of Xenopus early central nervous system development. The results reveal an unsuspected role for the prorenin receptor, V-ATPase activity, and acidification during Wnt/beta-catenin signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cruciat, Cristina-Maria -- Ohkawara, Bisei -- Acebron, Sergio P -- Karaulanov, Emil -- Reinhard, Carmen -- Ingelfinger, Dierk -- Boutros, Michael -- Niehrs, Christof -- New York, N.Y. -- Science. 2010 Jan 22;327(5964):459-63. doi: 10.1126/science.1179802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Embryology, DKFZ-ZMBH Alliance, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20093472" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; Cell Line ; Cell Line, Tumor ; Central Nervous System/cytology/embryology ; Embryo, Nonmammalian/metabolism ; Frizzled Receptors/metabolism ; Gene Expression Regulation, Developmental ; Homeodomain Proteins/genetics/metabolism ; Humans ; Hydrogen-Ion Concentration ; LDL-Receptor Related Proteins/metabolism ; Low Density Lipoprotein Receptor-Related Protein-6 ; Mice ; Nerve Tissue Proteins/genetics/metabolism ; Phosphorylation ; RNA, Small Interfering ; Receptors, Cell Surface/genetics/*metabolism ; *Signal Transduction ; Vacuolar Proton-Translocating ATPases/antagonists & inhibitors/*metabolism ; Wnt Proteins/*metabolism ; Wnt3 Protein ; Xenopus/embryology/metabolism ; Xenopus Proteins/genetics/*metabolism ; beta Catenin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-beta-catenin signaling (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-02-16
    Description: Casein kinase 1 (CK1) members play key roles in numerous biological processes. They are considered "rogue" kinases, because their enzymatic activity appears unregulated. Contrary to this notion, we have identified the DEAD-box RNA helicase DDX3 as a regulator of the Wnt-beta-catenin network, where it acts as a regulatory subunit of CK1epsilon: In a Wnt-dependent manner, DDX3 binds CK1epsilon and directly stimulates its kinase activity, and promotes phosphorylation of the scaffold protein dishevelled. DDX3 is required for Wnt-beta-catenin signaling in mammalian cells and during Xenopus and Caenorhabditis elegans development. The results also suggest that the kinase-stimulatory function extends to other DDX and CK1 members, opening fresh perspectives for one of the longest-studied protein kinase families.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cruciat, Cristina-Maria -- Dolde, Christine -- de Groot, Reinoud E A -- Ohkawara, Bisei -- Reinhard, Carmen -- Korswagen, Hendrik C -- Niehrs, Christof -- New York, N.Y. -- Science. 2013 Mar 22;339(6126):1436-41. doi: 10.1126/science.1231499. Epub 2013 Feb 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Embryology, DKFZ-ZMBH Alliance, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23413191" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Caenorhabditis elegans/genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins/genetics/metabolism ; Casein Kinase Iepsilon/chemistry/*metabolism ; DEAD-box RNA Helicases/chemistry/genetics/*metabolism ; HEK293 Cells ; Humans ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; RNA Helicases/chemistry/genetics/*metabolism ; Wnt Proteins/metabolism ; *Wnt Signaling Pathway ; Xenopus/embryology/genetics/metabolism ; Xenopus Proteins/chemistry/genetics/*metabolism ; beta Catenin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6 phosphorylation (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-16
    Description: Multiple signaling pathways, including Wnt signaling, participate in animal development, stem cell biology, and human cancer. Although many components of the Wnt pathway have been identified, unresolved questions remain as to the mechanism by which Wnt binding to its receptors Frizzled and Low-density lipoprotein receptor-related protein 6 (LRP6) triggers downstream signaling events. With live imaging of vertebrate cells, we show that Wnt treatment quickly induces plasma membrane-associated LRP6 aggregates. LRP6 aggregates are phosphorylated and can be detergent-solubilized as ribosome-sized multiprotein complexes. Phospho-LRP6 aggregates contain Wnt-pathway components but no common vesicular traffic markers except caveolin. The scaffold protein Dishevelled (Dvl) is required for LRP6 phosphorylation and aggregation. We propose that Wnts induce coclustering of receptors and Dvl in LRP6-signalosomes, which in turn triggers LRP6 phosphorylation to promote Axin recruitment and beta-catenin stabilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bilic, Josipa -- Huang, Ya-Lin -- Davidson, Gary -- Zimmermann, Timo -- Cruciat, Cristina-Maria -- Bienz, Mariann -- Niehrs, Christof -- MC_U105192713/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1619-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Embryology, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569865" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*metabolism ; Animals ; Axin Protein ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Centrifugation, Density Gradient ; Cytoplasm/metabolism ; Drosophila ; Glycogen Synthase Kinase 3/analysis/metabolism ; HeLa Cells ; Humans ; LDL-Receptor Related Proteins/analysis/genetics/*metabolism ; Low Density Lipoprotein Receptor-Related Protein-6 ; Mice ; Models, Biological ; Phosphoproteins/*metabolism ; Phosphorylation ; Repressor Proteins/analysis/metabolism ; *Signal Transduction ; Transfection ; Wnt Proteins/*metabolism ; Wnt3 Protein ; beta Catenin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc1 complex (1999)
    EMBO Press
    Details
    Publication Date: 1999-10-01
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
    Published by EMBO Press on behalf of European Molecular Biology Organization.
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