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  1. Article ; Online: Unfolding by Cdc48/p97: different strokes for different folks.

    Buchberger, Alexander

    Trends in cell biology

    2022  Volume 32, Issue 4, Page(s) 278–280

    Abstract: The protein unfoldase Cdc48/p97 targets a wide variety of cellular substrates, but the molecular basis of substrate turnover remains incompletely understood. Two recent reports, by Ji et al. and van den Boom et al., provide detailed insights into the ... ...

    Abstract The protein unfoldase Cdc48/p97 targets a wide variety of cellular substrates, but the molecular basis of substrate turnover remains incompletely understood. Two recent reports, by Ji et al. and van den Boom et al., provide detailed insights into the unfolding process and reveal pronounced flexibility of substrate handling by Cdc48/p97.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Humans ; Protein Folding ; Proteins/metabolism ; Valosin Containing Protein/chemistry ; Valosin Containing Protein/metabolism
    Chemical Substances Cell Cycle Proteins ; Proteins ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2022-01-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2022.01.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.MG 25: Show issues
    Zs.MO 113: Show issues
    Zs.A 3410: 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)

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  2. Article ; Online: Role of the Ubiquitin System in Stress Granule Metabolism.

    Tolay, Nazife / Buchberger, Alexander

    International journal of molecular sciences

    2022  Volume 23, Issue 7

    Abstract: Eukaryotic cells react to various stress conditions with the rapid formation of membrane-less organelles called stress granules (SGs). SGs form by multivalent interactions between RNAs and RNA-binding proteins and are believed to protect stalled ... ...

    Abstract Eukaryotic cells react to various stress conditions with the rapid formation of membrane-less organelles called stress granules (SGs). SGs form by multivalent interactions between RNAs and RNA-binding proteins and are believed to protect stalled translation initiation complexes from stress-induced degradation. SGs contain hundreds of different mRNAs and proteins, and their assembly and disassembly are tightly controlled by post-translational modifications. The ubiquitin system, which mediates the covalent modification of target proteins with the small protein ubiquitin ('ubiquitylation'), has been implicated in different aspects of SG metabolism, but specific functions in SG turnover have only recently emerged. Here, we summarize the evidence for the presence of ubiquitylated proteins at SGs, review the functions of different components of the ubiquitin system in SG formation and clearance, and discuss the link between perturbed SG clearance and the pathogenesis of neurodegenerative disorders. We conclude that the ubiquitin system plays an important, medically relevant role in SG biology.
    MeSH term(s) Cytoplasmic Granules/metabolism ; RNA-Binding Proteins/metabolism ; Stress Granules ; Stress, Physiological ; Ubiquitin/metabolism
    Chemical Substances RNA-Binding Proteins ; Ubiquitin
    Language English
    Publishing date 2022-03-26
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms23073624
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  3. Article ; Online: p97/VCP Promotes the Recycling of Endocytic Cargo.

    Kawan, Mona / Körner, Maria / Schlosser, Andreas / Buchberger, Alexander

    Molecular biology of the cell

    2023  Volume 34, Issue 13, Page(s) ar126

    Abstract: The endocytic pathway is of central importance for eukaryotic cells, as it enables uptake of extracellular materials, membrane protein quality control and recycling, as well as modulation of receptor signaling. While the ATPase p97 (VCP, Cdc48) has been ... ...

    Abstract The endocytic pathway is of central importance for eukaryotic cells, as it enables uptake of extracellular materials, membrane protein quality control and recycling, as well as modulation of receptor signaling. While the ATPase p97 (VCP, Cdc48) has been found to be involved in the fusion of early endosomes and endolysosomal degradation, its role in endocytic trafficking is still incompletely characterized. Here, we identify myoferlin (MYOF), a ferlin family member with functions in membrane trafficking and repair, as a hitherto unknown p97 interactor. The interaction of MYOF with p97 depends on the cofactor PLAA previously linked to endosomal sorting. Besides PLAA, shared interactors of p97 and MYOF comprise several proteins involved in endosomal recycling pathways, including Rab11, Rab14, and the transferrin receptor CD71. Accordingly, a fraction of p97 and PLAA localizes to MYOF-, Rab11-, and Rab14-positive endosomal compartments. Pharmacological inhibition of p97 delays transferrin recycling, indicating that p97 promotes not only the lysosomal degradation, but also the recycling of endocytic cargo.
    MeSH term(s) Biological Transport ; Endosomes/metabolism ; Membrane Proteins/metabolism ; Protein Transport ; Transferrin/metabolism ; Humans
    Chemical Substances Membrane Proteins ; Transferrin ; VCP protein, human (EC 3.6.4.6)
    Language English
    Publishing date 2023-09-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E23-06-0237
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: 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 410: Show issues

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  4. Article ; Online: Comparative profiling of stress granule clearance reveals differential contributions of the ubiquitin system.

    Tolay, Nazife / Buchberger, Alexander

    Life science alliance

    2021  Volume 4, Issue 5

    Abstract: Stress granules (SGs) are cytoplasmic condensates containing untranslated mRNP complexes. They are induced by various proteotoxic conditions such as heat, oxidative, and osmotic stress. SGs are believed to protect mRNPs from degradation and to enable ... ...

    Abstract Stress granules (SGs) are cytoplasmic condensates containing untranslated mRNP complexes. They are induced by various proteotoxic conditions such as heat, oxidative, and osmotic stress. SGs are believed to protect mRNPs from degradation and to enable cells to rapidly resume translation when stress conditions subside. SG dynamics are controlled by various posttranslational modifications, but the role of the ubiquitin system has remained controversial. Here, we present a comparative analysis addressing the involvement of the ubiquitin system in SG clearance. Using high-resolution immunofluorescence microscopy, we found that ubiquitin associated to varying extent with SGs induced by heat, arsenite, H
    MeSH term(s) Cytoplasmic Granules/metabolism ; Cytoplasmic Granules/physiology ; HeLa Cells ; Heat-Shock Response/physiology ; Humans ; Osmotic Pressure/physiology ; Oxidative Stress/physiology ; Stress, Physiological/genetics ; Stress, Physiological/physiology ; Ubiquitin/metabolism ; Ubiquitination/genetics ; Ubiquitination/physiology
    Chemical Substances Ubiquitin
    Language English
    Publishing date 2021-03-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202000927
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: ERQC autophagy: Yet another way to die.

    Buchberger, Alexander

    Molecular cell

    2014  Volume 54, Issue 1, Page(s) 3–4

    Abstract: A novel autophagy pathway eliminates nonnative polytopic membrane proteins from the endoplasmic reticulum that evade degradation by the ubiquitin proteasome system. ...

    Abstract A novel autophagy pathway eliminates nonnative polytopic membrane proteins from the endoplasmic reticulum that evade degradation by the ubiquitin proteasome system.
    MeSH term(s) Animals ; Autophagy ; Cytosol/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Eukaryotic Cells/metabolism ; Humans ; Protein Folding ; Proteins/metabolism ; Receptors, LHRH/metabolism
    Chemical Substances GNRHR protein, human ; Proteins ; Receptors, LHRH
    Language English
    Publishing date 2014-04-10
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2014.03.037
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: 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)

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  6. Article: Roles of Cdc48 in regulated protein degradation in yeast.

    Buchberger, Alexander

    Sub-cellular biochemistry

    2013  Volume 66, Page(s) 195–222

    Abstract: The chaperone-related, ubiquitin-selective AAA (ATPase associated with a variety of cellular activities) protein Cdc48 (also known as TER94, p97 and VCP) is a key regulator of intracellular proteolysis in eukaryotes. It uses the energy derived from ATP ... ...

    Abstract The chaperone-related, ubiquitin-selective AAA (ATPase associated with a variety of cellular activities) protein Cdc48 (also known as TER94, p97 and VCP) is a key regulator of intracellular proteolysis in eukaryotes. It uses the energy derived from ATP hydrolysis to segregate ubiquitylated proteins from stable assemblies with proteins, membranes and chromatin. Originally characterized as essential factor in proteasomal degradation pathways, Cdc48 was recently found to control lysosomal protein degradation as well. Moreover, impaired lysosomal proteolysis due to mutational inactivation of Cdc48 causes protein aggregation diseases in humans. This review introduces the major systems of intracellular proteolysis in eukaryotes and the role of protein ubiquitylation. It then discusses in detail structure, mechanism and cellular functions of Cdc48 with an emphasis on protein degradation pathways in yeast.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Cell Cycle Proteins/metabolism ; Proteolysis ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Valosin Containing Protein
    Chemical Substances Cell Cycle Proteins ; Saccharomyces cerevisiae Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; CDC48 protein, S cerevisiae (EC 3.6.4.-) ; VCP protein, human (EC 3.6.4.6) ; Valosin Containing Protein (EC 3.6.4.6)
    Language English
    Publishing date 2013
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-94-007-5940-4_8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Book ; Online ; Thesis: USP 10 als Deubiquitinase für β-Catenin

    Christmann, Gabriel [Verfasser] / Buchberger, Alexander [Gutachter] / Wiegering, Armin [Gutachter]

    2022  

    Author's details Gabriel Christmann ; Gutachter: Alexander Buchberger, Armin Wiegering
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universität Würzburg
    Publishing place Würzburg
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  8. Article ; Online: An unusual mode of baseline translation adjusts cellular protein synthesis capacity to metabolic needs.

    Schneider, Cornelius / Erhard, Florian / Binotti, Beyenech / Buchberger, Alexander / Vogel, Jörg / Fischer, Utz

    Cell reports

    2022  Volume 41, Issue 2, Page(s) 111467

    Abstract: In all domains of life, mechanisms exist that adjust translational capacity to nutrient restriction and other growth constraints. The mammalian target of rapamycin (mTOR) regulates the synthesis of ribosomal proteins and translation factors in mammalian ... ...

    Abstract In all domains of life, mechanisms exist that adjust translational capacity to nutrient restriction and other growth constraints. The mammalian target of rapamycin (mTOR) regulates the synthesis of ribosomal proteins and translation factors in mammalian cells via phosphorylation of the La-related protein 1 (LARP1). In the present model of starvation-induced translational silencing, LARP1 targets mRNAs carrying a 5' terminal oligopyrimidine (5'TOP) motif to shift these into subpolysomal ribonucleoprotein particles. However, how these mRNAs would be protected from degradation and rapidly made available to restore translation capacity when needed remained enigmatic. Here, to address this, we employ gradient profiling by sequencing (Grad-seq) and monosome footprinting. Challenging the above model, we find that 5'TOP mRNAs, instead of being translationally silenced during starvation, undergo low baseline translation with reduced initiation rates. This mode of regulation ensures a stable 5'TOP mRNA population under starvation and allows fast reversibility of the translational repression.
    MeSH term(s) Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Ribonucleoproteins/metabolism ; Ribosomal Proteins/metabolism ; TOR Serine-Threonine Kinases/metabolism
    Chemical Substances RNA, Messenger ; Ribonucleoproteins ; Ribosomal Proteins ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2022-10-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2022.111467
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Control of ubiquitin conjugation by cdc48 and its cofactors.

    Buchberger, Alexander

    Sub-cellular biochemistry

    2010  Volume 54, Page(s) 17–30

    Abstract: Cdc48 (alias p97, VCP) is an important motor and regulator for the turnover of ubiquitylated proteins, both in proteasomal degradation and in nonproteolytic pathways. The diverse cellular tasks of Cdc48 are controlled by a large number of cofactors. ... ...

    Abstract Cdc48 (alias p97, VCP) is an important motor and regulator for the turnover of ubiquitylated proteins, both in proteasomal degradation and in nonproteolytic pathways. The diverse cellular tasks of Cdc48 are controlled by a large number of cofactors. Substrate-recruiting cofactors mediate the specific recognition of ubiquitylated target proteins, whereas substrate-processing cofactors often exhibit ubiquitin ligase or deubiquitylating activities that enable them to modulate the ubiquitylation state of substrates. This chapter introduces the major groups of Cdc48 cofactors and discusses the versatile options of substrate-processing cofactors to control the fate of Cdc48 substrates.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Cell Cycle Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Cell Cycle Proteins ; Ubiquitin ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2010
    Publishing country United States
    Document type Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-1-4419-6676-6_2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: ERQC Autophagy: Yet Another Way to Die

    Buchberger, Alexander

    Molecular cell. 2014 Apr. 10, v. 54

    2014  

    Abstract: A novel autophagy pathway eliminates nonnative polytopic membrane proteins from the endoplasmic reticulum that evade degradation by the ubiquitin proteasome system. ...

    Abstract A novel autophagy pathway eliminates nonnative polytopic membrane proteins from the endoplasmic reticulum that evade degradation by the ubiquitin proteasome system.
    Keywords autophagy ; endoplasmic reticulum ; membrane proteins ; proteasome endopeptidase complex ; ubiquitin
    Language English
    Dates of publication 2014-0410
    Size p. 3-4.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2014.03.037
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

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