LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 66

Search options

  1. Article ; Online: Substrate selection by the proteasome through initiation regions.

    Tomita, Takuya / Matouschek, Andreas

    Protein science : a publication of the Protein Society

    2019  Volume 28, Issue 7, Page(s) 1222–1232

    Abstract: Proteins in the cell have to be eliminated once their function is no longer desired or they become damaged. Most regulated protein degradation is achieved by a large enzymatic complex called the proteasome. Many proteasome substrates are targeted for ... ...

    Abstract Proteins in the cell have to be eliminated once their function is no longer desired or they become damaged. Most regulated protein degradation is achieved by a large enzymatic complex called the proteasome. Many proteasome substrates are targeted for degradation by the covalent attachment of ubiquitin molecules. Ubiquitinated proteins can be bound by the proteasome, but for proteolysis to occur the proteasome needs to find a disordered tail somewhere in the target at which it initiates degradation. The initiation step contributes to the specificity of proteasomal degradation. Here, we review how the proteasome selects initiation sites within its substrates and discuss how the initiation step affects physiological processes.
    MeSH term(s) Animals ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Substrate Specificity ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2019-05-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.3642
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3407: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 1: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Senataxin deficiency disrupts proteostasis through nucleolar ncRNA-driven protein aggregation.

    Wen, Xuemei / Xu, Hengyi / Woolley, Phillip R / Conway, Olivia M / Yao, Jun / Matouschek, Andreas / Lambowitz, Alan M / Paull, Tanya T

    The Journal of cell biology

    2024  Volume 223, Issue 7

    Abstract: Senataxin is an evolutionarily conserved RNA-DNA helicase involved in DNA repair and transcription termination that is associated with human neurodegenerative disorders. Here, we investigated whether Senataxin loss affects protein homeostasis based on ... ...

    Abstract Senataxin is an evolutionarily conserved RNA-DNA helicase involved in DNA repair and transcription termination that is associated with human neurodegenerative disorders. Here, we investigated whether Senataxin loss affects protein homeostasis based on previous work showing R-loop-driven accumulation of DNA damage and protein aggregates in human cells. We find that Senataxin loss results in the accumulation of insoluble proteins, including many factors known to be prone to aggregation in neurodegenerative disorders. These aggregates are located primarily in the nucleolus and are promoted by upregulation of non-coding RNAs expressed from the intergenic spacer region of ribosomal DNA. We also map sites of R-loop accumulation in human cells lacking Senataxin and find higher RNA-DNA hybrids within the ribosomal DNA, peri-centromeric regions, and other intergenic sites but not at annotated protein-coding genes. These findings indicate that Senataxin loss affects the solubility of the proteome through the regulation of transcription-dependent lesions in the nucleus and the nucleolus.
    MeSH term(s) Humans ; Multifunctional Enzymes/metabolism ; Multifunctional Enzymes/genetics ; RNA Helicases/metabolism ; RNA Helicases/genetics ; Cell Nucleolus/metabolism ; Cell Nucleolus/genetics ; Proteostasis/genetics ; DNA Helicases/metabolism ; DNA Helicases/genetics ; RNA, Untranslated/genetics ; RNA, Untranslated/metabolism ; Protein Aggregates ; R-Loop Structures/genetics ; DNA Damage ; DNA, Ribosomal/genetics ; DNA, Ribosomal/metabolism
    Chemical Substances SETX protein, human (EC 3.6.1.-) ; Multifunctional Enzymes ; RNA Helicases (EC 3.6.4.13) ; DNA Helicases (EC 3.6.4.-) ; RNA, Untranslated ; Protein Aggregates ; DNA, Ribosomal
    Language English
    Publishing date 2024-05-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202309036
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.190: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: A masked initiation region in retinoblastoma protein regulates its proteasomal degradation.

    Tomita, Takuya / Huibregtse, Jon M / Matouschek, Andreas

    Nature communications

    2020  Volume 11, Issue 1, Page(s) 2019

    Abstract: Retinoblastoma protein (Rb) is a tumor suppressor that binds and represses E2F transcription factors. In cervical cancer cells, human papilloma virus (HPV) protein E7 binds to Rb, releasing it from E2F to promote cell cycle progression, and inducing ... ...

    Abstract Retinoblastoma protein (Rb) is a tumor suppressor that binds and represses E2F transcription factors. In cervical cancer cells, human papilloma virus (HPV) protein E7 binds to Rb, releasing it from E2F to promote cell cycle progression, and inducing ubiquitination of Rb. E7-mediated proteasomal degradation of Rb requires action by another protease, calpain, which cleaves Rb after Lys 810. However, it is not clear why cleavage is required for Rb degradation. Here, we report that the proteasome cannot initiate degradation efficiently on full-length Rb. Calpain cleavage exposes a region that is recognized by the proteasome, leading to rapid proteolysis of Rb. These findings identify a mechanism for regulating protein stability by controlling initiation and provide a better understanding of the molecular mechanism underlying transformation by HPV.
    MeSH term(s) Acrylates/pharmacology ; Calpain/antagonists & inhibitors ; Calpain/metabolism ; Cell Cycle/genetics ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/pathology ; Cyclopentanes/pharmacology ; E2F Transcription Factors/genetics ; E2F Transcription Factors/metabolism ; Female ; Gene Expression Regulation, Neoplastic ; HEK293 Cells ; Human papillomavirus 16/metabolism ; Human papillomavirus 16/pathogenicity ; Humans ; NEDD8 Protein/antagonists & inhibitors ; NEDD8 Protein/metabolism ; Oligopeptides/pharmacology ; Papillomavirus E7 Proteins/metabolism ; Proteasome Endopeptidase Complex/drug effects ; Proteasome Endopeptidase Complex/metabolism ; Protein Stability/drug effects ; Pyrimidines/pharmacology ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Retinoblastoma Binding Proteins/genetics ; Retinoblastoma Binding Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination/drug effects ; Ubiquitination/genetics ; Uterine Cervical Neoplasms/genetics ; Uterine Cervical Neoplasms/pathology ; Uterine Cervical Neoplasms/virology
    Chemical Substances Acrylates ; Cyclopentanes ; E2F Transcription Factors ; NEDD8 Protein ; NEDD8 protein, human ; Oligopeptides ; PD 150606 ; Papillomavirus E7 Proteins ; Pyrimidines ; RB1 protein, human ; Recombinant Proteins ; Retinoblastoma Binding Proteins ; oncogene protein E7, Human papillomavirus type 16 ; carfilzomib (72X6E3J5AR) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Calpain (EC 3.4.22.-) ; CAPN1 protein, human (EC 3.4.22.52) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; pevonedistat (S3AZD8D215)
    Language English
    Publishing date 2020-04-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-020-16003-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Mechanisms of substrate recognition by the 26S proteasome.

    Davis, Caroline / Spaller, Brian Logan / Matouschek, Andreas

    Current opinion in structural biology

    2020  Volume 67, Page(s) 161–169

    Abstract: The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitination, ...

    Abstract The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitination, and degradation is initiated at a disordered region within the protein. The ability of the proteasome to precisely select which proteins to break down is necessary for cellular functioning. Recent studies reveal the subtle mechanisms of substrate recognition by the proteasome - diverse ubiquitin chains can act as potent proteasome targeting signals, ubiquitin receptors function uniquely and cooperatively, and modification of initiation regions modulate degradation. Here, we summarize recent findings illuminating the nature of substrate recognition by the proteasome.
    MeSH term(s) Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; ATP dependent 26S protease (EC 3.4.99.-)
    Language English
    Publishing date 2020-12-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2020.10.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3206: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: A strict requirement in proteasome substrates for spacing between ubiquitin tag and degradation initiation elements.

    Davis, Caroline / Spaller, B L / Choi, Erin / Kurrasch, Joseph / Chong, Haemin / Elsasser, Suzanne / Finley, Daniel / Matouschek, Andreas

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Proteins are typically targeted to the proteasome for degradation through the attachment of ubiquitin chains and the proteasome initiates degradation at a disordered region within the target protein. Yet some proteins with ubiquitin chains and disordered ...

    Abstract Proteins are typically targeted to the proteasome for degradation through the attachment of ubiquitin chains and the proteasome initiates degradation at a disordered region within the target protein. Yet some proteins with ubiquitin chains and disordered regions escape degradation. Here we investigate how the position of the ubiquitin chain on the target protein relative to the disordered region modulates degradation and show that the distance between the two determines whether a protein is degraded efficiently. This distance depends on the type of the degradation tag and is likely a result of the separation on the proteasome between the receptor that binds the tag and the site that engages the disordered region.
    Language English
    Publishing date 2023-08-09
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.08.552540
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article ; Online: Recognition of Client Proteins by the Proteasome.

    Yu, Houqing / Matouschek, Andreas

    Annual review of biophysics

    2017  Volume 46, Page(s) 149–173

    Abstract: The ubiquitin proteasome system controls the concentrations of regulatory proteins and removes damaged and misfolded proteins from cells. Proteins are targeted to the protease at the center of this system, the proteasome, by ubiquitin tags, but ubiquitin ...

    Abstract The ubiquitin proteasome system controls the concentrations of regulatory proteins and removes damaged and misfolded proteins from cells. Proteins are targeted to the protease at the center of this system, the proteasome, by ubiquitin tags, but ubiquitin is also used as a signal in other cellular processes. Specificity is conferred by the size and structure of the ubiquitin tags, which are recognized by receptors associated with the different cellular processes. However, the ubiquitin code remains ambiguous, and the same ubiquitin tag can target different proteins to different fates. After binding substrate protein at the ubiquitin tag, the proteasome initiates degradation at a disordered region in the substrate. The proteasome has pronounced preferences for the initiation site, and its recognition represents a second component of the degradation signal.
    MeSH term(s) Humans ; Models, Molecular ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Proteins/chemistry ; Proteins/genetics ; Proteins/metabolism ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Proteins ; Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2017-03-09
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2434725-5
    ISSN 1936-1238 ; 1936-122X
    ISSN (online) 1936-1238
    ISSN 1936-122X
    DOI 10.1146/annurev-biophys-070816-033719
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Se 190: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Stability of 20S Proteasome Configurations: Preopening the Axial Gate.

    Henderson, Lucas W / Sharon, Edie M / Gautam, Amit K S / Anthony, Adam J / Jarrold, Martin F / Russell, David H / Matouschek, Andreas / Clemmer, David E

    The journal of physical chemistry letters

    2023  Volume 14, Issue 21, Page(s) 5014–5017

    Abstract: Mass spectrometry studies of the stability of ... ...

    Abstract Mass spectrometry studies of the stability of the
    MeSH term(s) Proteasome Endopeptidase Complex/chemistry ; Proteasome Endopeptidase Complex/metabolism ; Saccharomyces cerevisiae/metabolism ; Proteolysis
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2023-05-24
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.3c01040
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  8. Article ; Online: Decoding without the cipher.

    Singh Gautam, Amit Kumar / Matouschek, Andreas

    Nature chemical biology

    2019  Volume 15, Issue 3, Page(s) 210–212

    MeSH term(s) Genetic Code ; Sumoylation ; Ubiquitination
    Language English
    Publishing date 2019-04-08
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-019-0230-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6251: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 90: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Correction to "CDMS Analysis of Intact 19S, 20S, 26S, and 30S Proteasomes: Evidence for Higher-Order 20S Assemblies at a Low pH".

    Anthony, Adam J / Gautam, Amit K S / Miller, Lohra M / Ma, Yiran / Hardwick, Anya G / Sharma, Anu / Ghatak, Subhadip / Matouschek, Andreas / Jarrold, Martin F / Clemmer, David E

    Analytical chemistry

    2024  Volume 96, Issue 5, Page(s) 2273

    Language English
    Publishing date 2024-01-25
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.4c00103
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4033: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: An Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome Adaptors.

    Wilmington, Shameika R / Matouschek, Andreas

    PloS one

    2016  Volume 11, Issue 4, Page(s) e0152679

    Abstract: A common way to study protein function is to deplete the protein of interest from cells and observe the response. Traditional methods involve disrupting gene expression but these techniques are only effective against newly synthesized proteins and leave ... ...

    Abstract A common way to study protein function is to deplete the protein of interest from cells and observe the response. Traditional methods involve disrupting gene expression but these techniques are only effective against newly synthesized proteins and leave previously existing and stable proteins untouched. Here, we introduce a technique that induces the rapid degradation of specific proteins in mammalian cells by shuttling the proteins to the proteasome for degradation in a ubiquitin-independent manner. We present two implementations of the system in human culture cells that can be used individually to control protein concentration. Our study presents a simple, robust, and flexible technology platform for manipulating intracellular protein levels.
    MeSH term(s) Gene Expression ; HEK293 Cells ; Humans ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Ubiquitin/genetics ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2016-04-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0152679
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top