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  1. Article ; Online: TDP-43 Toxicity in Yeast Is Associated with a Reduction in Autophagy, and Deletions of

    Park, Sei-Kyoung / Park, Sangeun / Liebman, Susan W

    Viruses

    2022  Volume 14, Issue 10

    Abstract: When human TDP-43 is overexpressed in yeast it is toxic and forms cytoplasmic aggregates. The mechanism of this toxicity is unknown. Genetic screens for TDP-43 toxicity modifiers in the yeast system previously identified proteins, including PBP1, that ... ...

    Abstract When human TDP-43 is overexpressed in yeast it is toxic and forms cytoplasmic aggregates. The mechanism of this toxicity is unknown. Genetic screens for TDP-43 toxicity modifiers in the yeast system previously identified proteins, including PBP1, that enhance TDP-43 toxicity. The determination in yeast that deletion of
    MeSH term(s) Humans ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Autophagy/genetics ; Carrier Proteins/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Carrier Proteins ; DNA-Binding Proteins ; PBP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; TARDBP protein, human
    Language English
    Publishing date 2022-10-15
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14102264
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  2. Article ; Online: A founder mutation in FLNC is likely a major cause of idiopathic dilated cardiomyopathy in Ashkenazi Jews.

    Liebman, Susan W / Palaganas, Haley / Kobany, Haviva

    International journal of cardiology

    2020  Volume 323, Page(s) 124

    MeSH term(s) Cardiomyopathy, Dilated/diagnostic imaging ; Cardiomyopathy, Dilated/genetics ; Filamins/genetics ; Gene Frequency ; Humans ; Jews/genetics ; Mutation
    Chemical Substances FLNC protein, human ; Filamins
    Language English
    Publishing date 2020-08-15
    Publishing country Netherlands
    Document type Letter ; Comment
    ZDB-ID 779519-1
    ISSN 1874-1754 ; 0167-5273
    ISSN (online) 1874-1754
    ISSN 0167-5273
    DOI 10.1016/j.ijcard.2020.08.052
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1673: Show issues Location:
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  3. Article: Respiration Enhances TDP-43 Toxicity, but TDP-43 Retains Some Toxicity in the Absence of Respiration

    Park, Sei-Kyoung / Park, Sangeun / Liebman, Susan W

    Journal of molecular biology. 2019 May 03, v. 431, no. 10

    2019  

    Abstract: The trans-activating response DNA-binding protein 43 (TDP-43) is a transcriptional repressor and splicing factor. TDP-43 is normally mostly in the nucleus, although it shuttles to the cytoplasm. Mutations in TDP-43 are one cause of familial amyotrophic ... ...

    Abstract The trans-activating response DNA-binding protein 43 (TDP-43) is a transcriptional repressor and splicing factor. TDP-43 is normally mostly in the nucleus, although it shuttles to the cytoplasm. Mutations in TDP-43 are one cause of familial amyotrophic lateral sclerosis. In neurons of these patients, TDP-43 forms cytoplasmic aggregates. In addition, wild-type TDP-43 is also frequently found in neuronal cytoplasmic aggregates in patients with neurodegenerative diseases not caused by TDP-43 mutations. TDP-43 expressed in yeast causes toxicity and forms cytoplasmic aggregates. This disease model has been validated because genetic modifiers of TDP-43 toxicity in yeast have led to the discovery that their conserved genes in humans are amyotrophic lateral sclerosis genetic risk factors. While how TDP-43 is associated with toxicity is unknown, several studies find that TDP-43 alters mitochondrial function. We now report that TDP-43 is much more toxic when yeast are respiring than when grown on a carbon source where respiration is inhibited. However, respiration is not the unique target of TDP-43 toxicity because we found that TDP-43 retains some toxicity even in the absence of respiration. We found that H2O2 increases the toxicity of TDP-43, suggesting that the reactive oxygen species associated with respiration could likewise enhance the toxicity of TDP-43. In this case, the TDP-43 toxicity targets in the presence or absence of respiration could be identical, with the reactive oxygen species produced by respiration activating TDP-43 to become more toxic or making TDP-43 targets more vulnerable.
    Keywords amyotrophic lateral sclerosis ; carbon ; disease models ; genes ; humans ; hydrogen peroxide ; mitochondria ; mutation ; neurons ; patients ; repressor proteins ; risk factors ; toxicity ; yeasts
    Language English
    Dates of publication 2019-0503
    Size p. 2050-2059.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.03.014
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  4. Article ; Online: Respiration Enhances TDP-43 Toxicity, but TDP-43 Retains Some Toxicity in the Absence of Respiration.

    Park, Sei-Kyoung / Park, Sangeun / Liebman, Susan W

    Journal of molecular biology

    2019  Volume 431, Issue 10, Page(s) 2050–2059

    Abstract: The trans-activating response DNA-binding protein 43 (TDP-43) is a transcriptional repressor and splicing factor. TDP-43 is normally mostly in the nucleus, although it shuttles to the cytoplasm. Mutations in TDP-43 are one cause of familial amyotrophic ... ...

    Abstract The trans-activating response DNA-binding protein 43 (TDP-43) is a transcriptional repressor and splicing factor. TDP-43 is normally mostly in the nucleus, although it shuttles to the cytoplasm. Mutations in TDP-43 are one cause of familial amyotrophic lateral sclerosis. In neurons of these patients, TDP-43 forms cytoplasmic aggregates. In addition, wild-type TDP-43 is also frequently found in neuronal cytoplasmic aggregates in patients with neurodegenerative diseases not caused by TDP-43 mutations. TDP-43 expressed in yeast causes toxicity and forms cytoplasmic aggregates. This disease model has been validated because genetic modifiers of TDP-43 toxicity in yeast have led to the discovery that their conserved genes in humans are amyotrophic lateral sclerosis genetic risk factors. While how TDP-43 is associated with toxicity is unknown, several studies find that TDP-43 alters mitochondrial function. We now report that TDP-43 is much more toxic when yeast are respiring than when grown on a carbon source where respiration is inhibited. However, respiration is not the unique target of TDP-43 toxicity because we found that TDP-43 retains some toxicity even in the absence of respiration. We found that H
    MeSH term(s) Amyotrophic Lateral Sclerosis/metabolism ; Cell Respiration ; DNA-Binding Proteins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Oxidative Stress ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism
    Chemical Substances DNA-Binding Proteins ; Protein Aggregates ; TARDBP protein, human ; Hydrogen Peroxide (BBX060AN9V)
    Language English
    Publishing date 2019-03-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.03.014
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
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  5. Article ; Online: Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.

    Park, Sei-Kyoung / Park, Sangeun / Pentek, Christine / Liebman, Susan W

    iScience

    2020  Volume 24, Issue 1, Page(s) 102000

    Abstract: Mutations in the p53 tumor suppressor are frequent causes of cancer. Because p53 aggregates appear in some tumor cells, it has been suggested that p53 could also cause cancer by forming self-replicating protein aggregates (prions). Here, using yeast, we ... ...

    Abstract Mutations in the p53 tumor suppressor are frequent causes of cancer. Because p53 aggregates appear in some tumor cells, it has been suggested that p53 could also cause cancer by forming self-replicating protein aggregates (prions). Here, using yeast, we show that transient p53 overexpression induced the formation of p53 prion aggregates that were transmitted for >100 generations, found in lysate pellets, stained with Thioflavin T, and transmitted by cytoplasmic transfer, or transfection with lysates of cells carrying the prion or with p53 amyloid peptide. As predicted for a prion, transient interruption of p53 expression caused permanent p53 prion loss. Importantly, p53 transcription factor activity was reduced by prion formation suggesting that prion aggregation could cause cancer. p53 has also been found in liquid-like nuclear droplets in animal cell culture. In yeast, we found that liquid-like p53 foci appear in response to stress and disappear with stress removal.
    Language English
    Publishing date 2020-12-29
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2020.102000
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  6. Article ; Online: Prions and amyloids--an overview.

    Liebman, Susan W

    Seminars in cell & developmental biology

    2011  Volume 22, Issue 5, Page(s) 435–436

    MeSH term(s) Amyloid/metabolism ; Guidelines as Topic ; Humans ; Prions/metabolism
    Chemical Substances Amyloid ; Prions
    Language English
    Publishing date 2011-04-09
    Publishing country England
    Document type Editorial ; Introductory Journal Article
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2011.04.001
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2918: Show issues Location:
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  7. Article ; Online: Long non-coding RNA NEAT1_1 ameliorates TDP-43 toxicity in in vivo models of TDP-43 proteinopathy.

    Matsukawa, Koji / Kukharsky, Michail S / Park, Sei-Kyoung / Park, Sangeun / Watanabe, Naruaki / Iwatsubo, Takeshi / Hashimoto, Tadafumi / Liebman, Susan W / Shelkovnikova, Tatyana A

    RNA biology

    2021  Volume 18, Issue 11, Page(s) 1546–1554

    Abstract: Pathological changes involving TDP-43 protein ('TDP-43 proteinopathy') are typical for several neurodegenerative diseases, including frontotemporal lobar degeneration (FTLD). FTLD-TDP cases are characterized by increased binding of TDP-43 to an abundant ... ...

    Abstract Pathological changes involving TDP-43 protein ('TDP-43 proteinopathy') are typical for several neurodegenerative diseases, including frontotemporal lobar degeneration (FTLD). FTLD-TDP cases are characterized by increased binding of TDP-43 to an abundant lncRNA, NEAT1, in the cortex. However it is unclear whether enhanced TDP-43-NEAT1 interaction represents a protective mechanism. We show that accumulation of human TDP-43 leads to upregulation of the constitutive NEAT1 isoform, NEAT1_1, in cultured cells and in the brains of transgenic mice. Further, we demonstrate that overexpression of NEAT1_1 ameliorates TDP-43 toxicity in
    MeSH term(s) Amyotrophic Lateral Sclerosis/etiology ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Amyotrophic Lateral Sclerosis/prevention & control ; Animals ; Brain/metabolism ; Brain/pathology ; DNA-Binding Proteins/toxicity ; Disease Models, Animal ; Drosophila melanogaster ; Frontotemporal Dementia/etiology ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Frontotemporal Dementia/prevention & control ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neuroblastoma/etiology ; Neuroblastoma/metabolism ; Neuroblastoma/pathology ; Neuroblastoma/prevention & control ; RNA, Long Noncoding/administration & dosage ; RNA, Long Noncoding/genetics ; Saccharomyces cerevisiae ; TDP-43 Proteinopathies/etiology ; TDP-43 Proteinopathies/metabolism ; TDP-43 Proteinopathies/pathology ; TDP-43 Proteinopathies/prevention & control
    Chemical Substances DNA-Binding Proteins ; NEAT1 long non-coding RNA, human ; RNA, Long Noncoding ; TARDBP protein, human
    Language English
    Publishing date 2021-01-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2159587-2
    ISSN 1555-8584 ; 1555-8584
    ISSN (online) 1555-8584
    ISSN 1555-8584
    DOI 10.1080/15476286.2020.1860580
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  8. Article ; Online: The story of stolen chaperones: how overexpression of Q/N proteins cures yeast prions.

    Derkatch, Irina L / Liebman, Susan W

    Prion

    2013  Volume 7, Issue 4, Page(s) 294–300

    Abstract: Prions are self-seeding alternate protein conformations. Most yeast prions contain glutamine/asparagine (Q/N)-rich domains that promote the formation of amyloid-like prion aggregates. Chaperones, including Hsp104 and Sis1, are required to continually ... ...

    Abstract Prions are self-seeding alternate protein conformations. Most yeast prions contain glutamine/asparagine (Q/N)-rich domains that promote the formation of amyloid-like prion aggregates. Chaperones, including Hsp104 and Sis1, are required to continually break these aggregates into smaller "seeds." Decreasing aggregate size and increasing the number of growing aggregate ends facilitates both aggregate transmission and growth. Our previous work showed that overexpression of 11 proteins with Q/N-rich domains facilitates the de novo aggregation of Sup35 into the [PSI(+)] prion, presumably by a cross-seeding mechanism. We now discuss our recent paper, in which we showed that overexpression of most of these same 11 Q/N-rich proteins, including Pin4C and Cyc8, destabilized pre-existing Q/N rich prions. Overexpression of both Pin4C and Cyc8 caused [PSI(+)] aggregates to enlarge. This is incompatible with a previously proposed "capping" model where the overexpressed Q/N-rich protein poisons, or "caps," the growing aggregate ends. Rather the data match what is expected of a reduction in prion severing by chaperones. Indeed, while Pin4C overexpression does not alter chaperone levels, Pin4C aggregates sequester chaperones away from the prion aggregates. Cyc8 overexpression cures [PSI(+)] by inducing an increase in Hsp104 levels, as excess Hsp104 binds to [PSI(+)] aggregates in a way that blocks their shearing.
    MeSH term(s) Asparagine ; Molecular Chaperones ; Prions ; Protein Structure, Tertiary ; Saccharomyces cerevisiae
    Chemical Substances Molecular Chaperones ; Prions ; Asparagine (7006-34-0)
    Language English
    Publishing date 2013-08-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review ; Comment
    ZDB-ID 2267671-5
    ISSN 1933-690X ; 1933-690X
    ISSN (online) 1933-690X
    ISSN 1933-690X
    DOI 10.4161/pri.26021
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  9. Article: Variant-specific prion interactions: Complicating factors.

    Sharma, Jaya / Liebman, Susan W

    Cellular logistics

    2013  Volume 3, Issue 1, Page(s) e25698

    Abstract: Prions are protein conformations that "self-seed" the misfolding of their non-prion iso-forms into prion, often amyloid, conformations. The most famous prion is the mammalian PrP protein that in its prion form causes transmissible spongiform ... ...

    Abstract Prions are protein conformations that "self-seed" the misfolding of their non-prion iso-forms into prion, often amyloid, conformations. The most famous prion is the mammalian PrP protein that in its prion form causes transmissible spongiform encephalopathy. Curiously there can be distinct conformational differences even between prions of the same protein propagated in the same host species. These are called prion strains or variants. For example, different PrP variants are faithfully transmitted during self-seeding and are associated with distinct disease characteristics. Variant-specific PrP prion differences include the length of the incubation period before the disease appears and the deposition of prion aggregates in distinct regions of the brain.
    Language English
    Publishing date 2013-09-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2682440-1
    ISSN 2159-2799 ; 2159-2780
    ISSN (online) 2159-2799
    ISSN 2159-2780
    DOI 10.4161/cl.25698
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  10. Article ; Online: Retrospective. Fred Sherman (1932-2013).

    Liebman, Susan W / Haber, James E

    Science (New York, N.Y.)

    2013  Volume 342, Issue 6162, Page(s) 1059

    MeSH term(s) Genetics/history ; History, 20th Century ; History, 21st Century ; Saccharomyces cerevisiae/genetics ; United States
    Language English
    Publishing date 2013-11-29
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portraits
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.1248055
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 27: Show issues Location:
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    Zs.MG 77: Show issues

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