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  1. Article ; Online: Differential Interactions of the Proteasome Inhibitor PI31 with Constitutive and Immuno-20S Proteasomes.

    Wang, Jason / Kjellgren, Abbey / DeMartino, George N

    Biochemistry

    2024  Volume 63, Issue 8, Page(s) 1000–1015

    Abstract: PI31 ( ...

    Abstract PI31 (
    MeSH term(s) Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors/pharmacology ; Cryoelectron Microscopy ; Proteins/chemistry ; Cytoplasm/metabolism ; Antiviral Agents
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Proteasome Inhibitors ; Proteins ; Antiviral Agents
    Language English
    Publishing date 2024-04-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.3c00707
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  2. Article ; Online: 2019 Herbert Tabor Young Investigator Awards: Call for nominations.

    DeMartino, George N

    The Journal of biological chemistry

    2018  Volume 293, Issue 37, Page(s) 14571

    Language English
    Publishing date 2018-09-14
    Publishing country United States
    Document type Editorial
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.E118.005617
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  3. Article ; Online: Introduction to the Thematic Minireview Series: Autophagy.

    DeMartino, George N

    The Journal of biological chemistry

    2018  Volume 293, Issue 15, Page(s) 5384–5385

    Abstract: Autophagy is a highly conserved, tightly regulated cellular process that degrades intracellular constituents via lysosomes. Autophagy mediates many normal cellular functions and is dysregulated in numerous diseases. This Thematic Series consists of five ... ...

    Abstract Autophagy is a highly conserved, tightly regulated cellular process that degrades intracellular constituents via lysosomes. Autophagy mediates many normal cellular functions and is dysregulated in numerous diseases. This Thematic Series consists of five Minireviews that highlight selected topics of current autophagy research ranging from the molecular mechanisms and regulation of autophagy to the roles of autophagy in health and disease.
    MeSH term(s) Animals ; Autophagy ; Humans
    Language English
    Publishing date 2018-02-21
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.TM118.002429
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  4. Article: High-resolution structure of mammalian PI31â€"20S proteasome complex reveals mechanism of proteasome inhibition.

    Hsu, Hao-Chi / Wang, Jason / Kjellgren, Abbey / Li, Huilin / DeMartino, George N

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Proteasome-catalyzed protein degradation mediates and regulates critical aspects of many cellular functions and is an important element of proteostasis in health and disease. Proteasome function is determined in part by the types of proteasome ... ...

    Abstract Proteasome-catalyzed protein degradation mediates and regulates critical aspects of many cellular functions and is an important element of proteostasis in health and disease. Proteasome function is determined in part by the types of proteasome holoenzymes formed between the 20S core particle that catalyzes peptide bond hydrolysis and any of multiple regulatory proteins to which it binds. One of these regulators, PI31, was previously identified as an
    Language English
    Publishing date 2023-04-07
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.04.03.535455
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  5. Article ; Online: Ηigh-resolution structure of mammalian PI31-20S proteasome complex reveals mechanism of proteasome inhibition.

    Hsu, Hao-Chi / Wang, Jason / Kjellgren, Abbey / Li, Huilin / DeMartino, George N

    The Journal of biological chemistry

    2023  Volume 299, Issue 7, Page(s) 104862

    Abstract: Proteasome-catalyzed protein degradation mediates and regulates critical aspects of many cellular functions and is an important element of proteostasis in health and disease. Proteasome function is determined in part by the types of proteasome ... ...

    Abstract Proteasome-catalyzed protein degradation mediates and regulates critical aspects of many cellular functions and is an important element of proteostasis in health and disease. Proteasome function is determined in part by the types of proteasome holoenzymes formed between the 20S core particle that catalyzes peptide bond hydrolysis and any of multiple regulatory proteins to which it binds. One of these regulators, PI31, was previously identified as an in vitro 20S proteasome inhibitor, but neither the molecular mechanism nor the possible physiologic significance of PI31-mediated proteasome inhibition has been clear. Here we report a high-resolution cryo-EM structure of the mammalian 20S proteasome in complex with PI31. The structure shows that two copies of the intrinsically disordered carboxyl terminus of PI31 are present in the central cavity of the closed-gate conformation of the proteasome and interact with proteasome catalytic sites in a manner that blocks proteolysis of substrates but resists their own degradation. The two inhibitory polypeptide chains appear to originate from PI31 monomers that enter the catalytic chamber from opposite ends of the 20S cylinder. We present evidence that PI31 can inhibit proteasome activity in mammalian cells and may serve regulatory functions for the control of cellular proteostasis.
    MeSH term(s) Animals ; Proteasome Endopeptidase Complex/metabolism ; Cytoplasm/metabolism ; Proteolysis ; Proteostasis ; Mammals/metabolism
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2023-05-25
    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 10.1016/j.jbc.2023.104862
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  6. Article ; Online: 2021 JBC Herbert Tabor Early Career Investigator Awards: Call for nominations.

    Gierasch, Lila M / DeMartino, George N

    The Journal of biological chemistry

    2020  Volume 295, Issue 39, Page(s) 13697

    Language English
    Publishing date 2020-11-20
    Publishing country United States
    Document type Editorial
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.E120.015888
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  7. Article ; Online: 2020 Herbert Tabor Early Career Investigator Awards: Call for nominations.

    Gierasch, Lila M / DeMartino, George N

    The Journal of biological chemistry

    2019  Volume 294, Issue 36, Page(s) 13526

    MeSH term(s) Awards and Prizes ; Humans ; Periodicals as Topic ; Research ; United States
    Language English
    Publishing date 2019-09-05
    Publishing country United States
    Document type Editorial
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.E119.010739
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  8. Article ; Online: Mimicking Protein Kinase C Phosphorylation Inhibits Arc/Arg3.1 Palmitoylation and Its Interaction with Nucleic Acids.

    Barylko, Barbara / Taylor, Clinton A / Wang, Jason / Earnest, Svetlana / Stippec, Steve / Binns, Derk D / Brautigam, Chad A / Jameson, David M / DeMartino, George N / Cobb, Melanie H / Albanesi, Joseph P

    International journal of molecular sciences

    2024  Volume 25, Issue 2

    Abstract: ... within an α-helical segment in the N-terminal domain. To mimic the effect of PKC phosphorylation, we mutated ...

    Abstract Activity-regulated cytoskeleton-associated protein (Arc) plays essential roles in diverse forms of synaptic plasticity, including long-term potentiation (LTP), long-term depression (LTD), and homeostatic plasticity. In addition, it assembles into virus-like particles that may deliver mRNAs and/or other cargo between neurons and neighboring cells. Considering this broad range of activities, it is not surprising that Arc is subject to regulation by multiple types of post-translational modification, including phosphorylation, palmitoylation, SUMOylation, ubiquitylation, and acetylation. Here we explore the potential regulatory role of Arc phosphorylation by protein kinase C (PKC), which occurs on serines 84 and 90 within an α-helical segment in the N-terminal domain. To mimic the effect of PKC phosphorylation, we mutated the two serines to negatively charged glutamic acid. A consequence of introducing these phosphomimetic mutations is the almost complete inhibition of Arc palmitoylation, which occurs on nearby cysteines and contributes to synaptic weakening. The mutations also inhibit the binding of nucleic acids and destabilize high-order Arc oligomers. Thus, PKC phosphorylation of Arc may limit the full expression of LTD and may suppress the interneuronal transport of mRNAs.
    MeSH term(s) Phosphorylation ; Lipoylation ; Nucleic Acids ; Protein Processing, Post-Translational ; Protein Kinase C/genetics
    Chemical Substances Nucleic Acids ; Protein Kinase C (EC 2.7.11.13)
    Language English
    Publishing date 2024-01-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25020780
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  9. Article ; Online: Reconstitution of PA700, the 19S regulatory particle, from purified precursor complexes.

    Demartino, George N

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

    2012  Volume 832, Page(s) 443–452

    Abstract: Here, we describe methodology for the in vitro reconstitution of PA700, the 19S regulatory particle of the 26S proteasome, from three purified subcomplexes that closely represent cellular assembly intermediates. These PA700 subcomplexes (denoted PS-1, PS- ...

    Abstract Here, we describe methodology for the in vitro reconstitution of PA700, the 19S regulatory particle of the 26S proteasome, from three purified subcomplexes that closely represent cellular assembly intermediates. These PA700 subcomplexes (denoted PS-1, PS-2, and PS-3) account for all subunits present in purified PA700 but have no overlapping or non-PA700 components. The reconstituted PA700 displays functional features indistinguishable from independently purified PA700, including ATPase activity, deubiquitylating activity, and ATP-dependent binding and activation of the 20S proteasome. This reconstitution assay -provides a platform for exploration of critical biochemical and molecular features of PA700 assembly and for insights to 26S proteasome assembly in intact cells.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Erythrocytes/enzymology ; Humans ; Proteasome Endopeptidase Complex/analysis ; Proteasome Endopeptidase Complex/biosynthesis ; Proteasome Endopeptidase Complex/chemistry ; Proteasome Endopeptidase Complex/metabolism ; Protein Structure, Tertiary
    Chemical Substances PA700 proteasome activator ; Adenosine Triphosphate (8L70Q75FXE) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-)
    Language English
    Publishing date 2012-02-19
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-61779-474-2_31
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  10. Article ; Online: Highly conserved shifts in ubiquitin-proteasome system (UPS) activity drive mitochondrial remodeling during quiescence.

    Yue, Sibiao / Wang, Lei / DeMartino, George N / Zhao, FangZhou / Liu, Yi / Sieber, Matthew H

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 4462

    Abstract: Defects in cellular proteostasis and mitochondrial function drive many aspects of infertility, cancer, and other age-related diseases. All of these conditions rely on quiescent cells, such as oocytes and adult stem cells, that reduce their activity and ... ...

    Abstract Defects in cellular proteostasis and mitochondrial function drive many aspects of infertility, cancer, and other age-related diseases. All of these conditions rely on quiescent cells, such as oocytes and adult stem cells, that reduce their activity and remain dormant as part of their roles in tissue homeostasis, reproduction, and even cancer recurrence. Using a multi-organism approach, we show that dynamic shifts in the ubiquitin proteasome system drive mitochondrial remodeling during cellular quiescence. In contrast to the commonly held view that the ubiquitin-proteasome system (UPS) is primarily regulated by substrate ubiquitination, we find that increasing proteasome number and their recruitment to mitochondria support mitochondrial respiratory quiescence (MRQ). GSK3 triggers proteasome recruitment to the mitochondria by phosphorylating outer membrane proteins, such as VDAC, and suppressing mitochondrial fatty acid oxidation. This work defines a process that couples dynamic regulation of UPS activity to coordinated shifts in mitochondrial metabolism in fungi, Drosophila, and mammals during quiescence.
    MeSH term(s) Animals ; Glycogen Synthase Kinase 3/metabolism ; Mammals/metabolism ; Mitochondria/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2022-08-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-32206-2
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