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  1. Book ; Online ; Thesis: Functional validation of Alzheimer’s disease risk genes using established and pluripotent human cell culture models

    Rudolph, Ina-Maria [Verfasser]

    2019  

    Author's details Ina-Maria Rudolph
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Freie Universität Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  2. Article ; Online: Corrigendum to Flemming J, Marczenke M, Rudolph I-M, et al. Induced pluripotent stem cell-based disease modeling identifies ligand-induced decay of megalin as a cause of Donnai-Barrow syndrome. Kidney Int. 2020;98:159-167.

    Flemming, Julia / Marczenke, Maike / Rudolph, Ina-Maria / Nielsen, Rikke / Storm, Tina / Ilsoe Christensen, Erik / Diecke, Sebastian / Emma, Francesco / Willnow, Thomas E

    Kidney international

    2021  Volume 100, Issue 2, Page(s) 482

    Language English
    Publishing date 2021-07-22
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2021.06.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Risk factor SORL1: from genetic association to functional validation in Alzheimer's disease.

    Andersen, Olav M / Rudolph, Ina-Maria / Willnow, Thomas E

    Acta neuropathologica

    2016  Volume 132, Issue 5, Page(s) 653–665

    Abstract: Alzheimer's disease (AD) represents one of the most dramatic threats to healthy aging and devising effective treatments for this devastating condition remains a major challenge in biomedical research. Much has been learned about the molecular concepts ... ...

    Abstract Alzheimer's disease (AD) represents one of the most dramatic threats to healthy aging and devising effective treatments for this devastating condition remains a major challenge in biomedical research. Much has been learned about the molecular concepts that govern proteolytic processing of the amyloid precursor protein to amyloid-β peptides (Aβ), and how accelerated accumulation of neurotoxic Aβ peptides underlies neuronal cell death in rare familial but also common sporadic forms of this disease. Out of a plethora of proposed modulators of amyloidogenic processing, one protein emerged as a key factor in AD pathology, a neuronal sorting receptor termed SORLA. Independent approaches using human genetics, clinical pathology, or exploratory studies in animal models all converge on this receptor that is now considered a central player in AD-related processes by many. This review will provide a comprehensive overview of the evidence implicating SORLA-mediated protein sorting in neurodegenerative processes, and how receptor gene variants in the human population impair functional receptor expression in sporadic but possibly also in autosomal-dominant forms of AD.
    MeSH term(s) Alzheimer Disease/genetics ; Animals ; Disease Models, Animal ; Genetic Variation/genetics ; Humans ; LDL-Receptor Related Proteins/genetics ; Membrane Transport Proteins/genetics ; Risk Factors
    Chemical Substances LDL-Receptor Related Proteins ; Membrane Transport Proteins ; SORL1 protein, human
    Language English
    Publishing date 2016-09-16
    Publishing country Germany
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1079-0
    ISSN 1432-0533 ; 0001-6322
    ISSN (online) 1432-0533
    ISSN 0001-6322
    DOI 10.1007/s00401-016-1615-4
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  4. Article ; Online: Induced pluripotent stem cell-based disease modeling identifies ligand-induced decay of megalin as a cause of Donnai-Barrow syndrome.

    Flemming, Julia / Marczenke, Maike / Rudolph, Ina-Maria / Nielsen, Rikke / Storm, Tina / Erik, Ilsoe Christensen / Diecke, Sebastian / Emma, Francesco / Willnow, Thomas E

    Kidney international

    2020  Volume 98, Issue 1, Page(s) 159–167

    Abstract: Donnai-Barrow syndrome (DBS) is an autosomal-recessive disorder characterized by multiple pathologies including malformation of forebrain and eyes, as well as resorption defects of the kidney proximal tubule. The underlying cause of DBS are mutations in ... ...

    Abstract Donnai-Barrow syndrome (DBS) is an autosomal-recessive disorder characterized by multiple pathologies including malformation of forebrain and eyes, as well as resorption defects of the kidney proximal tubule. The underlying cause of DBS are mutations in LRP2, encoding the multifunctional endocytic receptor megalin. Here, we identified a unique missense mutation R3192Q of LRP2 in an affected family that may provide novel insights into the molecular causes of receptor dysfunction in the kidney proximal tubule and other tissues affected in DBS. Using patient-derived induced pluripotent stem cell lines we generated neuroepithelial and kidney cell types as models of the disease. Using these cell models, we documented the inability of megalin R3192Q to properly discharge ligand and ligand-induced receptor decay in lysosomes. Thus, mutant receptors are aberrantly targeted to lysosomes for catabolism, essentially depleting megalin in the presence of ligand in this affected family.
    MeSH term(s) Agenesis of Corpus Callosum ; Endocytosis ; Hearing Loss, Sensorineural ; Hernias, Diaphragmatic, Congenital ; Humans ; Induced Pluripotent Stem Cells ; Kidney Tubules, Proximal ; Ligands ; Low Density Lipoprotein Receptor-Related Protein-2/genetics ; Myopia ; Proteinuria ; Renal Tubular Transport, Inborn Errors
    Chemical Substances Ligands ; Low Density Lipoprotein Receptor-Related Protein-2
    Language English
    Publishing date 2020-03-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120573-0
    ISSN 1523-1755 ; 0085-2538
    ISSN (online) 1523-1755
    ISSN 0085-2538
    DOI 10.1016/j.kint.2020.02.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: A complex of the ubiquitin ligase TRIM32 and the deubiquitinase USP7 balances the level of c-Myc ubiquitination and thereby determines neural stem cell fate specification.

    Nicklas, Sarah / Hillje, Anna-Lena / Okawa, Satoshi / Rudolph, Ina-Maria / Collmann, Franziska Melanie / van Wuellen, Thea / Del Sol, Antonio / Schwamborn, Jens C

    Cell death and differentiation

    2018  Volume 26, Issue 4, Page(s) 728–740

    Abstract: The balance between stem cell maintenance and differentiation has been proposed to depend on antagonizing ubiquitination and deubiquitination reactions of key stem cell transcription factors (SCTFs) mediated by pairs of E3 ubiquitin ligases and ... ...

    Abstract The balance between stem cell maintenance and differentiation has been proposed to depend on antagonizing ubiquitination and deubiquitination reactions of key stem cell transcription factors (SCTFs) mediated by pairs of E3 ubiquitin ligases and deubiquitinating enzymes. Accordingly, increased ubiquitination results in proteasomal degradation of the SCTF, thereby inducing cellular differentiation, whereas increased deubiquitination stabilizes the SCTF, leading to maintenance of the stem cell fate. In neural stem cells, one of the key SCTFs is c-Myc. Previously, it has been shown that c-Myc is ubiquitinated by the E3 ligase TRIM32, thereby targeting c-Myc for proteasomal degradation and inducing neuronal differentiation. Accordingly, TRIM32 becomes upregulated during adult neurogenesis. This upregulation is accompanied by subcellular translocation of TRIM32 from the cytoplasm of neuroblasts to the nucleus of neurons. However, we observed that a subpopulation of proliferative type C cells already contains nuclear TRIM32. As these cells do not undergo neuronal differentiation, despite containing TRIM32 in the nucleus, where it can ubiquitinate c-Myc, we hypothesize that antagonizing factors, specifically deubiquitinating enzymes, are present in these particular cells. Here we show that TRIM32 associates with the deubiquitination enzyme USP7, which previously has been implicated in neural stem cell maintenance. USP7 and TRIM32 were found to exhibit a dynamic and partially overlapping expression pattern during neuronal differentiation both in vitro and in vivo. Most importantly, we are able to demonstrate that USP7 deubiquitinates and thereby stabilizes c-Myc and that this function is required to maintain neural stem cell fate. Accordingly, we propose the balanced ubiquitination and deubiquitination of c-Myc by TRIM32 and USP7 as a novel mechanism for stem cell fate determination.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Cell Proliferation/genetics ; Cells, Cultured ; Gene Ontology ; HEK293 Cells ; Humans ; Lateral Ventricles/metabolism ; Mice ; Mice, Inbred C57BL ; Neural Stem Cells/enzymology ; Neural Stem Cells/metabolism ; Neurogenesis/genetics ; Neurons/metabolism ; Protein Processing, Post-Translational ; Proto-Oncogene Proteins c-myc/antagonists & inhibitors ; Proto-Oncogene Proteins c-myc/genetics ; Proto-Oncogene Proteins c-myc/metabolism ; Ubiquitin-Protein Ligases/antagonists & inhibitors ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitin-Specific Peptidase 7/antagonists & inhibitors ; Ubiquitin-Specific Peptidase 7/genetics ; Ubiquitin-Specific Peptidase 7/metabolism ; Ubiquitination
    Chemical Substances Myc protein, mouse ; Proto-Oncogene Proteins c-myc ; TRIM32 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Ubiquitin-Specific Peptidase 7 (EC 3.4.19.12) ; Usp7 protein, mouse (EC 3.4.19.12)
    Language English
    Publishing date 2018-06-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1225672-9
    ISSN 1476-5403 ; 1350-9047
    ISSN (online) 1476-5403
    ISSN 1350-9047
    DOI 10.1038/s41418-018-0144-1
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  6. Article ; Online: Mutations in Disordered Regions Can Cause Disease by Creating Dileucine Motifs.

    Meyer, Katrina / Kirchner, Marieluise / Uyar, Bora / Cheng, Jing-Yuan / Russo, Giulia / Hernandez-Miranda, Luis R / Szymborska, Anna / Zauber, Henrik / Rudolph, Ina-Maria / Willnow, Thomas E / Akalin, Altuna / Haucke, Volker / Gerhardt, Holger / Birchmeier, Carmen / Kühn, Ralf / Krauss, Michael / Diecke, Sebastian / Pascual, Juan M / Selbach, Matthias

    Cell

    2018  Volume 175, Issue 1, Page(s) 239–253.e17

    Abstract: Many disease-causing missense mutations affect intrinsically disordered regions (IDRs) of proteins, but the molecular mechanism of their pathogenicity is enigmatic. Here, we employ a peptide-based proteomic screen to investigate the impact of mutations ... ...

    Abstract Many disease-causing missense mutations affect intrinsically disordered regions (IDRs) of proteins, but the molecular mechanism of their pathogenicity is enigmatic. Here, we employ a peptide-based proteomic screen to investigate the impact of mutations in IDRs on protein-protein interactions. We find that mutations in disordered cytosolic regions of three transmembrane proteins (GLUT1, ITPR1, and CACNA1H) lead to an increased clathrin binding. All three mutations create dileucine motifs known to mediate clathrin-dependent trafficking. Follow-up experiments on GLUT1 (SLC2A1), the glucose transporter causative of GLUT1 deficiency syndrome, revealed that the mutated protein mislocalizes to intracellular compartments. Mutant GLUT1 interacts with adaptor proteins (APs) in vitro, and knocking down AP-2 reverts the cellular mislocalization and restores glucose transport. A systematic analysis of other known disease-causing variants revealed a significant and specific overrepresentation of gained dileucine motifs in structurally disordered cytosolic domains of transmembrane proteins. Thus, several mutations in disordered regions appear to cause "dileucineopathies."
    MeSH term(s) Amino Acid Motifs/genetics ; Amino Acid Sequence ; Animals ; Binding Sites ; Calcium Channels, T-Type/genetics ; Calcium Channels, T-Type/physiology ; Carbohydrate Metabolism, Inborn Errors ; Clathrin/metabolism ; Cytoplasm/metabolism ; Glucose Transporter Type 1/genetics ; Glucose Transporter Type 1/metabolism ; Glucose Transporter Type 1/physiology ; Humans ; Inositol 1,4,5-Trisphosphate Receptors/genetics ; Inositol 1,4,5-Trisphosphate Receptors/physiology ; Intrinsically Disordered Proteins/genetics ; Intrinsically Disordered Proteins/metabolism ; Intrinsically Disordered Proteins/physiology ; Leucine/metabolism ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Monosaccharide Transport Proteins/deficiency ; Mutation/genetics ; Peptides ; Protein Binding ; Proteomics/methods
    Chemical Substances Cacna1h protein, mouse ; Calcium Channels, T-Type ; Clathrin ; Glucose Transporter Type 1 ; Inositol 1,4,5-Trisphosphate Receptors ; Intrinsically Disordered Proteins ; Itpr1 protein, mouse ; Membrane Proteins ; Monosaccharide Transport Proteins ; Peptides ; SLC2A1 protein, human ; Leucine (GMW67QNF9C)
    Language English
    Publishing date 2018-09-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2018.08.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: A systemic transcriptome analysis reveals the regulation of neural stem cell maintenance by an E2F1-miRNA feedback loop.

    Palm, Thomas / Hemmer, Kathrin / Winter, Julia / Fricke, Inga B / Tarbashevich, Katsiaryna / Sadeghi Shakib, Fereshteh / Rudolph, Ina-Maria / Hillje, Anna-Lena / De Luca, Paola / Bahnassawy, Lamia'a / Madel, Rabea / Viel, Thomas / De Siervi, Adriana / Jacobs, Andreas H / Diederichs, Sven / Schwamborn, Jens C

    Nucleic acids research

    2013  Volume 41, Issue 6, Page(s) 3699–3712

    Abstract: Stem cell fate decisions are controlled by a molecular network in which transcription factors and miRNAs are of key importance. To systemically investigate their impact on neural stem cell (NSC) maintenance and neuronal commitment, we performed a high- ... ...

    Abstract Stem cell fate decisions are controlled by a molecular network in which transcription factors and miRNAs are of key importance. To systemically investigate their impact on neural stem cell (NSC) maintenance and neuronal commitment, we performed a high-throughput mRNA and miRNA profiling and isolated functional interaction networks of involved mechanisms. Thereby, we identified an E2F1-miRNA feedback loop as important regulator of NSC fate decisions. Although E2F1 supports NSC proliferation and represses transcription of miRNAs from the miR-17∼92 and miR-106a∼363 clusters, these miRNAs are transiently up-regulated at early stages of neuronal differentiation. In these early committed cells, increased miRNAs expression levels directly repress E2F1 mRNA levels and inhibit cellular proliferation. In mice, we demonstrated that these miRNAs are expressed in the neurogenic areas and that E2F1 inhibition represses NSC proliferation. The here presented data suggest a novel interaction mechanism between E2F1 and miR-17∼92 / miR-106a∼363 miRNAs in controlling NSC proliferation and neuronal differentiation.
    MeSH term(s) Animals ; Cell Cycle/genetics ; Cells, Cultured ; E2F1 Transcription Factor/antagonists & inhibitors ; E2F1 Transcription Factor/metabolism ; Feedback, Physiological ; Gene Expression Profiling ; Gene Expression Regulation ; Mice ; MicroRNAs/biosynthesis ; MicroRNAs/metabolism ; Neural Stem Cells/metabolism ; Neurogenesis/genetics ; RNA, Messenger/metabolism
    Chemical Substances E2F1 Transcription Factor ; E2f1 protein, mouse ; MIRN17-92 microRNA, mouse ; MicroRNAs ; RNA, Messenger
    Language English
    Publishing date 2013-02-08
    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/gkt070
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