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  1. Book ; Thesis: Posttranslational regulation of the Wnt secretory pathway

    Gläser, Kathrin

    2017  

    Author's details presented by Dipl. Biochemist Kathrin Gläser
    Language English
    Size VIII, 152 Blätter, Illustrationen, Diagramme
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruperto-Carola University of Heidelberg, 2017
    Note Zusammenfassung in deutscher und englischer Sprache
    HBZ-ID HT019515501
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2017 E 1811 order for loan Magazin

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  2. Article ; Online: Biochemical Methods to Analyze Wnt Protein Secretion.

    Glaeser, Kathrin / Boutros, Michael / Gross, Julia Christina

    Methods in molecular biology (Clifton, N.J.)

    2016  Volume 1481, Page(s) 17–28

    Abstract: Wnt proteins act as potent morphogens in various aspects of embryonic development and adult tissue homeostasis. However, in addition to its physiological importance, aberrant Wnt signaling has been linked to the onset and progression of different types ... ...

    Abstract Wnt proteins act as potent morphogens in various aspects of embryonic development and adult tissue homeostasis. However, in addition to its physiological importance, aberrant Wnt signaling has been linked to the onset and progression of different types of cancer. On the cellular level, the secretion of Wnt proteins involves trafficking of lipid-modified Wnts from the endoplasmic reticulum (ER) to Golgi and further compartments via the Wnt cargo receptor evenness interrupted. Others and we have recently shown that Wnt proteins are secreted on extracellular vesicles (EVs) such as microvesicles and exosomes. Although more details about specific regulation of Wnt secretion steps are emerging, it remains largely unknown how Wnt proteins are channeled into different release pathways such as lipoprotein particles, EVs and cytonemes. Here, we describe protocols to purify and quantify Wnts from the supernatant of cells by either assessing total Wnt proteins in the supernatant or monitoring Wnt proteins on EVs. Purified Wnts from the supernatant as well as total cellular protein content can be investigated by immunoblotting. Additionally, the relative activity of canonical Wnts in the supernatant can be assessed by a dual-luciferase Wnt reporter assay. Quantifying the amount of secreted Wnt proteins and their activity in the supernatant of cells allows the investigation of intracellular trafficking events that regulate Wnt secretion and the role of extracellular modulators of Wnt spreading.
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-6393-5_3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: ERAD-dependent control of the Wnt secretory factor Evi.

    Glaeser, Kathrin / Urban, Manuela / Fenech, Emma / Voloshanenko, Oksana / Kranz, Dominique / Lari, Federica / Christianson, John C / Boutros, Michael

    The EMBO journal

    2018  Volume 37, Issue 4

    Abstract: Active regulation of protein abundance is an essential strategy to modulate cellular signaling pathways. Within the Wnt signaling cascade, regulated degradation of β-catenin by the ubiquitin-proteasome system (UPS) affects the outcome of canonical Wnt ... ...

    Abstract Active regulation of protein abundance is an essential strategy to modulate cellular signaling pathways. Within the Wnt signaling cascade, regulated degradation of β-catenin by the ubiquitin-proteasome system (UPS) affects the outcome of canonical Wnt signaling. Here, we found that abundance of the Wnt cargo receptor Evi (Wls/GPR177), which is required for Wnt protein secretion, is also regulated by the UPS through endoplasmic reticulum (ER)-associated degradation (ERAD). In the absence of Wnt ligands, Evi is ubiquitinated and targeted for ERAD in a VCP-dependent manner. Ubiquitination of Evi involves the E2-conjugating enzyme UBE2J2 and the E3-ligase CGRRF1. Furthermore, we show that a triaging complex of Porcn and VCP determines whether Evi enters the secretory or the ERAD pathway. In this way, ERAD-dependent control of Evi availability impacts the scale of Wnt protein secretion by adjusting the amount of Evi to meet the requirement of Wnt protein export. As Wnt and Evi protein levels are often dysregulated in cancer, targeting regulatory ERAD components might be a useful approach for therapeutic interventions.
    MeSH term(s) Acyltransferases/genetics ; Acyltransferases/metabolism ; Adenocarcinoma/genetics ; Adenocarcinoma/metabolism ; Cells, Cultured ; Colon/metabolism ; Colonic Neoplasms/genetics ; Colonic Neoplasms/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Gene Expression Regulation ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitination ; Valosin Containing Protein/genetics ; Valosin Containing Protein/metabolism ; Wnt Proteins/genetics ; Wnt Proteins/metabolism
    Chemical Substances Membrane Proteins ; Ubiquitin ; Wnt Proteins ; Acyltransferases (EC 2.3.-) ; PORCN protein, human (EC 2.3.1.-) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; VCP protein, human (EC 3.6.4.6) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2018-01-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.201797311
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: E-TALEN: a web tool to design TALENs for genome engineering.

    Heigwer, Florian / Kerr, Grainne / Walther, Nike / Glaeser, Kathrin / Pelz, Oliver / Breinig, Marco / Boutros, Michael

    Nucleic acids research

    2013  Volume 41, Issue 20, Page(s) e190

    Abstract: Use of transcription activator-like effector nucleases (TALENs) is a promising new technique in the field of targeted genome engineering, editing and reverse genetics. Its applications span from introducing knockout mutations to endogenous tagging of ... ...

    Abstract Use of transcription activator-like effector nucleases (TALENs) is a promising new technique in the field of targeted genome engineering, editing and reverse genetics. Its applications span from introducing knockout mutations to endogenous tagging of proteins and targeted excision repair. Owing to this wide range of possible applications, there is a need for fast and user-friendly TALEN design tools. We developed E-TALEN (http://www.e-talen.org), a web-based tool to design TALENs for experiments of varying scale. E-TALEN enables the design of TALENs against a single target or a large number of target genes. We significantly extended previously published design concepts to consider genomic context and different applications. E-TALEN guides the user through an end-to-end design process of de novo TALEN pairs, which are specific to a certain sequence or genomic locus. Furthermore, E-TALEN offers a functionality to predict targeting and specificity for existing TALENs. Owing to the computational complexity of many of the steps in the design of TALENs, particular emphasis has been put on the implementation of fast yet accurate algorithms. We implemented a user-friendly interface, from the input parameters to the presentation of results. An additional feature of E-TALEN is the in-built sequence and annotation database available for many organisms, including human, mouse, zebrafish, Drosophila and Arabidopsis, which can be extended in the future.
    MeSH term(s) Animals ; Binding Sites ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Deoxyribonucleases, Type II Site-Specific/chemistry ; Gene Targeting ; Genetic Engineering ; Genomics ; Humans ; Internet ; Mice ; Sequence Analysis, DNA ; Software
    Chemical Substances DNA-Binding Proteins ; endodeoxyribonuclease FokI (EC 3.1.21.-) ; Deoxyribonucleases, Type II Site-Specific (EC 3.1.21.4)
    Language English
    Publishing date 2013-09-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkt789
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.

    Neal, Sonya E / Dabir, Deepa V / Tienson, Heather L / Horn, Darryl M / Glaeser, Kathrin / Ogozalek Loo, Rachel R / Barrientos, Antoni / Koehler, Carla M

    The Journal of biological chemistry

    2015  Volume 290, Issue 34, Page(s) 20804–20814

    Abstract: A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. ... ...

    Abstract A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation. In this study, we have addressed the oxidation of Tim13 in vitro and in organello. Reductants such as glutathione and ascorbate inhibited both the oxidation of the substrate Tim13 in vitro and the import of Tim13 and Cmc1 into isolated mitochondria. In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro. Instead, Mia40 accepted six electrons from substrates, and this fully reduced Mia40 was sensitive to protease, indicative of conformational changes in the structure. Mia40 in mitochondria from the erv1-101 mutant was also trapped in a completely reduced state, demonstrating that Mia40 can accept up to six electrons as substrates are imported. Therefore, these studies support that Mia40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates.
    MeSH term(s) Ascorbic Acid/pharmacology ; Disulfides/chemistry ; Disulfides/metabolism ; Electrons ; Gene Expression Regulation, Fungal ; Glutathione/pharmacology ; Metallochaperones/genetics ; Metallochaperones/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Oxidation-Reduction ; Oxidoreductases Acting on Sulfur Group Donors/genetics ; Oxidoreductases Acting on Sulfur Group Donors/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Reducing Agents/pharmacology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
    Chemical Substances CMC1 protein, S cerevisiae ; Disulfides ; MIA40 protein, S cerevisiae ; Metallochaperones ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Recombinant Proteins ; Reducing Agents ; Saccharomyces cerevisiae Proteins ; TIM13 protein, S cerevisiae ; Oxidoreductases Acting on Sulfur Group Donors (EC 1.8.-) ; ERV1 protein, S cerevisiae (EC 1.8.3.2) ; Glutathione (GAN16C9B8O) ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2015-06-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M115.669440
    Database MEDical Literature Analysis and Retrieval System OnLINE

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