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  1. Article ; Online: Molecular Biology of Cytoplasmic Incompatibility Caused by

    Hochstrasser, Mark

    Annual review of microbiology

    2023  Volume 77, Page(s) 299–316

    Abstract: Among endosymbiotic bacteria living within eukaryotic cells, ...

    Abstract Among endosymbiotic bacteria living within eukaryotic cells,
    MeSH term(s) Female ; Male ; Humans ; Wolbachia/genetics ; Semen ; Reproduction/genetics ; Cytoplasm ; Molecular Biology ; Symbiosis
    Language English
    Publishing date 2023-06-07
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 207931-8
    ISSN 1545-3251 ; 0066-4227
    ISSN (online) 1545-3251
    ISSN 0066-4227
    DOI 10.1146/annurev-micro-041020-024616
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  2. Article ; Online: Cytoplasmic incompatibility: A Wolbachia toxin-antidote mechanism comes into view.

    Hochstrasser, Mark

    Current biology : CB

    2022  Volume 32, Issue 6, Page(s) R287–R289

    Abstract: The Wolbachia cidA and cidB genes promote bacterial endosymbiont inheritance through the host female germline. CidB is now shown to load into maturing sperm nuclei. Following fertilization, it disrupts paternal chromosome condensation, triggering ... ...

    Abstract The Wolbachia cidA and cidB genes promote bacterial endosymbiont inheritance through the host female germline. CidB is now shown to load into maturing sperm nuclei. Following fertilization, it disrupts paternal chromosome condensation, triggering embryonic arrest if not countered by CidA in Wolbachia-infected eggs.
    MeSH term(s) Animals ; Antidotes ; Cytoplasm ; Cytosol ; Drosophila melanogaster/genetics ; Wolbachia/genetics
    Chemical Substances Antidotes
    Language English
    Publishing date 2022-04-13
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2022.02.014
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  3. Article ; Online: Preface.

    Hochstrasser, Mark

    Methods in enzymology

    2019  Volume 618, Page(s) xvii–xix

    Language English
    Publishing date 2019-03-08
    Publishing country United States
    Document type Editorial
    ISSN 1557-7988 ; 0076-6879
    ISSN (online) 1557-7988
    ISSN 0076-6879
    DOI 10.1016/S0076-6879(19)30079-5
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  4. Article ; Online: Ectopic RING activity at the ER membrane differentially impacts ERAD protein quality control pathways.

    Mehrtash, Adrian B / Hochstrasser, Mark

    The Journal of biological chemistry

    2023  Volume 299, Issue 3, Page(s) 102927

    Abstract: Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway that ensures misfolded proteins are removed from the ER and destroyed. In ERAD, membrane and luminal substrates are ubiquitylated by ER-resident RING-type E3 ... ...

    Abstract Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway that ensures misfolded proteins are removed from the ER and destroyed. In ERAD, membrane and luminal substrates are ubiquitylated by ER-resident RING-type E3 ubiquitin ligases, retrotranslocated into the cytosol, and degraded by the proteasome. Overexpression of ERAD factors is frequently used in yeast and mammalian cells to study this process. Here, we analyze the impact of ERAD E3 overexpression on substrate turnover in yeast, where there are three ERAD E3 complexes (Doa10, Hrd1, and Asi1-3). Elevated Doa10 or Hrd1 (but not Asi1) RING activity at the ER membrane resulting from protein overexpression inhibits the degradation of specific Doa10 substrates. The ERAD E2 ubiquitin-conjugating enzyme Ubc6 becomes limiting under these conditions, and UBC6 overexpression restores Ubc6-mediated ERAD. Using a subset of the dominant-negative mutants, which contain the Doa10 RING domain but lack the E2-binding region, we show that they induce degradation of membrane tail-anchored Ubc6 independently of endogenous Doa10 and the other ERAD E3 complexes. This remains true even if the cells lack the Dfm1 rhomboid pseudoprotease, which is also a proposed retrotranslocon. Hence, rogue RING activity at the ER membrane elicits a highly specific off-pathway defect in the Doa10 pathway, and the data point to an additional ERAD E3-independent retrotranslocation mechanism.
    MeSH term(s) Endoplasmic Reticulum-Associated Degradation ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Gene Expression
    Chemical Substances Dfm1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2023-01-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.102927
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  5. Article ; Online: Preface.

    Hochstrasser, Mark

    Methods in enzymology

    2019  Volume 619, Page(s) xv–xvii

    MeSH term(s) Animals ; Endoplasmic Reticulum-Associated Degradation ; Enzyme Assays/methods ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Protein Transport ; Proteolysis ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2019-02-20
    Publishing country United States
    Document type Editorial ; Introductory Journal Article
    ISSN 1557-7988 ; 0076-6879
    ISSN (online) 1557-7988
    ISSN 0076-6879
    DOI 10.1016/S0076-6879(19)30113-2
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  6. Article ; Online: Elements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets.

    Mehrtash, Adrian B / Hochstrasser, Mark

    iScience

    2022  Volume 25, Issue 11, Page(s) 105351

    Abstract: In ER-associated degradation (ERAD), misfolded ER proteins are degraded by the proteasome after undergoing ubiquitylation. Yeast Doa10 (human MARCHF6/TEB4) is a membrane-embedded E3 ubiquitin ligase that functions with E2s Ubc6 and Ubc7. Ubc6 attaches a ... ...

    Abstract In ER-associated degradation (ERAD), misfolded ER proteins are degraded by the proteasome after undergoing ubiquitylation. Yeast Doa10 (human MARCHF6/TEB4) is a membrane-embedded E3 ubiquitin ligase that functions with E2s Ubc6 and Ubc7. Ubc6 attaches a single ubiquitin to substrates, which is extended by Ubc7 to form a polyubiquitin chain. We show the conserved C-terminal element (CTE) of Doa10 promotes E3-mediated Ubc6 activity. Doa10 substrates undergoing an alternative ubiquitylation mechanism are still degraded in CTE-mutant cells. Structure prediction by AlphaFold2 suggests the CTE binds near the catalytic RING-CH domain, implying a direct role in substrate ubiquitylation, and we confirm this interaction using intragenic suppression. Truncation analysis defines a minimal E2-binding region of Doa10; structural predictions suggest that Doa10 forms a retrotranslocation channel and that E2s bind within the cofactor-binding region defined here. These results provide mechanistic insight into how Doa10, and potentially other ligases, interact with their cofactors and mediate ERAD.
    Language English
    Publishing date 2022-10-13
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2022.105351
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  7. Article ; Online: Selective microautophagy of proteasomes is initiated by ESCRT-0 and is promoted by proteasome ubiquitylation.

    Li, Jianhui / Hochstrasser, Mark

    Journal of cell science

    2022  Volume 135, Issue 4

    Abstract: The proteasome is central to proteolysis by the ubiquitin-proteasome system under normal growth conditions but is itself degraded through macroautophagy under nutrient stress. A recently described AMP-activated protein kinase (AMPK)-regulated endosomal ... ...

    Abstract The proteasome is central to proteolysis by the ubiquitin-proteasome system under normal growth conditions but is itself degraded through macroautophagy under nutrient stress. A recently described AMP-activated protein kinase (AMPK)-regulated endosomal sorting complex required for transport (ESCRT)-dependent microautophagy pathway also regulates proteasome trafficking and degradation in low-glucose conditions in yeast. Aberrant proteasomes are more prone to microautophagy, suggesting the ESCRT system fine-tunes proteasome quality control under low-glucose stress. Here, we uncover additional features of the selective microautophagy of proteasomes in budding yeast. Genetic or pharmacological induction of aberrant proteasomes is associated with increased mono- or oligo-ubiquitylation of proteasome components, which appears to be recognized by ESCRT-0. AMPK controls this pathway in part by regulating the trafficking of ESCRT-0 to the vacuole surface, which also leads to degradation of the Vps27 subunit of ESCRT-0. The Rsp5 ubiquitin ligase contributes to proteasome subunit ubiquitylation, and multiple ubiquitin-binding elements in Vps27 are involved in their recognition. We propose that ESCRT-0 at the vacuole surface recognizes ubiquitylated proteasomes and initiates their microautophagic elimination during glucose depletion. This article has an associated First Person interview with the first author of the paper.
    MeSH term(s) Endosomal Sorting Complexes Required for Transport/metabolism ; Humans ; Microautophagy ; Proteasome Endopeptidase Complex/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Ubiquitination
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Saccharomyces cerevisiae Proteins ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2022-02-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.259393
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  8. Article ; Online: Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.

    Breckel, Carolyn Allain / Johnson, Zane M / Hickey, Christopher M / Hochstrasser, Mark

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 2048

    Abstract: In eukaryotes, the ubiquitin-proteasome system is an essential pathway for protein degradation and cellular homeostasis. 26S proteasomes concentrate in the nucleus of budding yeast Saccharomyces cerevisiae due to the essential import adaptor protein Sts1 ...

    Abstract In eukaryotes, the ubiquitin-proteasome system is an essential pathway for protein degradation and cellular homeostasis. 26S proteasomes concentrate in the nucleus of budding yeast Saccharomyces cerevisiae due to the essential import adaptor protein Sts1 and the karyopherin-α protein Srp1. Here, we show that Sts1 facilitates proteasome nuclear import by recruiting proteasomes to the karyopherin-α/β heterodimer. Following nuclear transport, the karyopherin proteins are likely separated from Sts1 through interaction with RanGTP in the nucleus. RanGTP-induced release of Sts1 from the karyopherin proteins initiates Sts1 proteasomal degradation in vitro. Sts1 undergoes karyopherin-mediated nuclear import in the absence of proteasome interaction, but Sts1 degradation in vivo is only observed when proteasomes successfully localize to the nucleus. Sts1 appears to function as a proteasome import factor during exponential growth only, as it is not found in proteasome storage granules (PSGs) during prolonged glucose starvation, nor does it appear to contribute to the rapid nuclear reimport of proteasomes following glucose refeeding and PSG dissipation. We propose that Sts1 acts as a single-turnover proteasome nuclear import factor by recruiting karyopherins for transport and undergoing subsequent RanGTP-initiated ubiquitin-independent proteasomal degradation in the nucleus.
    MeSH term(s) Active Transport, Cell Nucleus ; Adaptor Proteins, Signal Transducing ; alpha Karyopherins ; beta Karyopherins ; Glucose ; Karyopherins ; Proteasome Endopeptidase Complex ; Saccharomyces cerevisiae ; Saccharomycetales ; Ubiquitin
    Chemical Substances Adaptor Proteins, Signal Transducing ; alpha Karyopherins ; ATP dependent 26S protease (EC 3.4.99.-) ; beta Karyopherins ; Glucose (IY9XDZ35W2) ; Karyopherins ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Ubiquitin ; STS1 protein, S cerevisiae
    Language English
    Publishing date 2024-01-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-024-52352-5
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  9. Article ; Online: Proteasomes: Isolation and Activity Assays.

    Li, Yanjie / Tomko, Robert J / Hochstrasser, Mark

    Current protocols

    2023  Volume 3, Issue 4, Page(s) e717

    Abstract: In eukaryotes, damaged or unneeded proteins are typically degraded by the ubiquitin-proteasome system. In this system, the protein substrate is often first covalently modified with a chain of ubiquitin polypeptides. This chain serves as a signal for ... ...

    Abstract In eukaryotes, damaged or unneeded proteins are typically degraded by the ubiquitin-proteasome system. In this system, the protein substrate is often first covalently modified with a chain of ubiquitin polypeptides. This chain serves as a signal for delivery to the 26S proteasome, a 2.5-MDa, ATP-dependent multisubunit protease complex. The proteasome consists of a barrel-shaped 20S core particle (CP) that is capped on one or both of its ends by a 19S regulatory particle (RP). The RP is responsible for recognizing the substrate, unfolding it, and translocating it into the CP for destruction. Here we describe simple, one-step purification schemes for isolating the 26S proteasome and its 19S RP and 20S CP subcomplexes from the yeast Saccharomyces cerevisiae. A gel filtration step can be added to further enhance purity. We also describe assays for measuring ubiquitin-dependent and ubiquitin-independent proteolytic activity in vitro. © 2023 Wiley Periodicals LLC. Basic Protocol 1: Purification of active 26S proteasomes Support Protocol 1: Growth of yeast strains and production of yeast cell powder Support Protocol 2: Regeneration of anti-flag M2 affinity gel Basic Protocol 2: Purification of the 19S regulatory particle (RP) Basic Protocol 3: Purification of active 20S CP Basic Protocol 4: In-gel peptidase activity assay for 20S CP and 26S proteasomes Basic Protocol 5: In-solution peptidase activity assay for 20S and 26S proteasomes Basic Protocol 6: Measuring degradation of polyubiquitinated SIC1
    MeSH term(s) Proteasome Endopeptidase Complex/metabolism ; Saccharomyces cerevisiae/metabolism ; Ubiquitin ; Cytoplasm/metabolism ; Yeast, Dried
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Ubiquitin
    Language English
    Publishing date 2023-03-31
    Publishing country United States
    Document type Journal Article
    ISSN 2691-1299
    ISSN (online) 2691-1299
    DOI 10.1002/cpz1.717
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  10. Article ; Online: Gyre and gimble in the proteasome.

    Hochstrasser, Mark

    Proceedings of the National Academy of Sciences of the United States of America

    2016  Volume 113, Issue 46, Page(s) 12896–12898

    Language English
    Publishing date 2016-11-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1616055113
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