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  1. Article ; Online: Autophagosomes are formed at a distinct cellular structure.

    Hollenstein, David M / Kraft, Claudine

    Current opinion in cell biology

    2020  Volume 65, Page(s) 50–57

    Abstract: Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment ... ...

    Abstract Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment of the core autophagy machinery to distinct cellular sites, referred to as phagophore assembly sites (PAS) in yeast or autophagosome formation sites in other organisms. A large number of autophagy proteins involved in the formation of autophagosomes has been identified; however, how the individual components of the PAS are assembled and how they function to generate autophagosomes remains a fundamental question. Here, we highlight recent studies that provide molecular insights into PAS organization and the role of the endoplasmic reticulum and the vacuole in autophagosome formation.
    MeSH term(s) Autophagosomes/metabolism ; Autophagy ; Cells/metabolism ; Models, Biological ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2020-03-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2020.02.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
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  2. Article ; Online: GSE1 links the HDAC1/CoREST co-repressor complex to DNA damage.

    Vcelkova, Terezia / Reiter, Wolfgang / Zylka, Martha / Hollenstein, David M / Schuckert, Stefan / Hartl, Markus / Seiser, Christian

    Nucleic acids research

    2023  Volume 51, Issue 21, Page(s) 11748–11769

    Abstract: Post-translational modifications of histones are important regulators of the DNA damage response (DDR). By using affinity purification mass spectrometry (AP-MS) we discovered that genetic suppressor element 1 (GSE1) forms a complex with the HDAC1/CoREST ... ...

    Abstract Post-translational modifications of histones are important regulators of the DNA damage response (DDR). By using affinity purification mass spectrometry (AP-MS) we discovered that genetic suppressor element 1 (GSE1) forms a complex with the HDAC1/CoREST deacetylase/demethylase co-repressor complex. In-depth phosphorylome analysis revealed that loss of GSE1 results in impaired DDR, ATR signalling and γH2AX formation upon DNA damage induction. Altered profiles of ATR target serine-glutamine motifs (SQ) on DDR-related hallmark proteins point to a defect in DNA damage sensing. In addition, GSE1 knock-out cells show hampered DNA damage-induced phosphorylation on SQ motifs of regulators of histone post-translational modifications, suggesting altered histone modification. While loss of GSE1 does not affect the histone deacetylation activity of CoREST, GSE1 appears to be essential for binding of the deubiquitinase USP22 to CoREST and for the deubiquitination of H2B K120 in response to DNA damage. The combination of deacetylase, demethylase, and deubiquitinase activity makes the USP22-GSE1-CoREST subcomplex a multi-enzymatic eraser that seems to play an important role during DDR. Since GSE1 has been previously associated with cancer progression and survival our findings are potentially of high medical relevance.
    MeSH term(s) Cell Nucleus/metabolism ; Co-Repressor Proteins/metabolism ; Deubiquitinating Enzymes/genetics ; DNA Damage ; Histones/genetics ; Histones/metabolism ; Humans ; Animals ; Mice ; Cell Line
    Chemical Substances Co-Repressor Proteins ; Deubiquitinating Enzymes (EC 3.4.19.12) ; Histones ; GSE1 protein, human ; RCOR1 protein, human ; HDAC1 protein, human (EC 3.5.1.98)
    Language English
    Publishing date 2023-10-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad911
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Chemical Acetylation of Ligands and Two-Step Digestion Protocol for Reducing Codigestion in Affinity Purification-Mass Spectrometry.

    Hollenstein, David M / Maurer-Granofszky, Margarita / Reiter, Wolfgang / Anrather, Dorothea / Gossenreiter, Thomas / Babic, Riccardo / Hartl, Natascha / Kraft, Claudine / Hartl, Markus

    Journal of proteome research

    2023  Volume 22, Issue 10, Page(s) 3383–3391

    Abstract: We present an effective, fast, and user-friendly method to reduce codigestion of bead-bound ligands, such as antibodies or streptavidin, in affinity purification-mass spectrometry experiments. A short preincubation of beads with Sulfo-NHS-Acetate leads ... ...

    Abstract We present an effective, fast, and user-friendly method to reduce codigestion of bead-bound ligands, such as antibodies or streptavidin, in affinity purification-mass spectrometry experiments. A short preincubation of beads with Sulfo-NHS-Acetate leads to chemical acetylation of lysine residues, making ligands insusceptible to Lys-C-mediated proteolysis. In contrast to similar approaches, our procedure offers the advantage of exclusively using nontoxic chemicals and employing mild chemical reaction conditions. After binding of bait proteins to Sulfo-NHS-Acetate treated beads, we employ a two-step digestion protocol with the sequential use of Lys-C protease for on-bead digestion followed by in-solution digestion of the released proteins with trypsin. The implementation of this protocol results in a strong reduction of contaminating ligand peptides, which allows significantly higher amounts of sample to be subjected to LC-MS analysis, improving sensitivity and quantitative accuracy.
    Language English
    Publishing date 2023-09-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.3c00424
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Decoding the function of Atg13 phosphorylation reveals a role of Atg11 in bulk autophagy initiation.

    Bhattacharya, Anuradha / Torggler, Raffaela / Reiter, Wolfgang / Romanov, Natalie / Licheva, Mariya / Ciftci, Akif / Mari, Muriel / Kolb, Lena / Kaiser, Dominik / Reggiori, Fulvio / Ammerer, Gustav / Hollenstein, David M / Kraft, Claudine

    EMBO reports

    2024  Volume 25, Issue 2, Page(s) 813–831

    Abstract: Autophagy is initiated by the assembly of multiple autophagy-related proteins that form the phagophore assembly site where autophagosomes are formed. Atg13 is essential early in this process, and a hub of extensive phosphorylation. How these multiple ... ...

    Abstract Autophagy is initiated by the assembly of multiple autophagy-related proteins that form the phagophore assembly site where autophagosomes are formed. Atg13 is essential early in this process, and a hub of extensive phosphorylation. How these multiple phosphorylations contribute to autophagy initiation, however, is not well understood. Here we comprehensively analyze the role of phosphorylation events on Atg13 during nutrient-rich conditions and nitrogen starvation. We identify and functionally characterize 48 in vivo phosphorylation sites on Atg13. By generating reciprocal mutants, which mimic the dephosphorylated active and phosphorylated inactive state of Atg13, we observe that disrupting the dynamic regulation of Atg13 leads to insufficient or excessive autophagy, which are both detrimental to cell survival. We furthermore demonstrate an involvement of Atg11 in bulk autophagy even during nitrogen starvation, where it contributes together with Atg1 to the multivalency that drives phase separation of the phagophore assembly site. These findings reveal the importance of post-translational regulation on Atg13 early during autophagy initiation, which provides additional layers of regulation to control bulk autophagy activity and integrate cellular signals.
    MeSH term(s) Phosphorylation ; Autophagy/physiology ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Signal Transduction ; Nitrogen ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Autophagy-Related Proteins ; Nitrogen (N762921K75) ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2024-01-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.1038/s44319-023-00055-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5433: Show issues Location:
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    Zs.MG 41: Show issues

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  5. Article ; Online: Spatial control of avidity regulates initiation and progression of selective autophagy.

    Hollenstein, David M / Licheva, Mariya / Konradi, Nicole / Schweida, David / Mancilla, Hector / Mari, Muriel / Reggiori, Fulvio / Kraft, Claudine

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 7194

    Abstract: Autophagosomes form at the endoplasmic reticulum in mammals, and between the vacuole and the endoplasmic reticulum in yeast. However, the roles of these sites and the mechanisms regulating autophagosome formation are incompletely understood. Vac8 is ... ...

    Abstract Autophagosomes form at the endoplasmic reticulum in mammals, and between the vacuole and the endoplasmic reticulum in yeast. However, the roles of these sites and the mechanisms regulating autophagosome formation are incompletely understood. Vac8 is required for autophagy and recruits the Atg1 kinase complex to the vacuole. Here we show that Vac8 acts as a central hub to nucleate the phagophore assembly site at the vacuolar membrane during selective autophagy. Vac8 directly recruits the cargo complex via the Atg11 scaffold. In addition, Vac8 recruits the phosphatidylinositol 3-kinase complex independently of autophagy. Cargo-dependent clustering and Vac8-dependent sequestering of these early autophagy factors, along with local Atg1 activation, promote phagophore assembly site assembly at the vacuole. Importantly, ectopic Vac8 redirects autophagosome formation to the nuclear membrane, indicating that the vacuolar membrane is not specifically required. We propose that multiple avidity-driven interactions drive the initiation and progression of selective autophagy.
    MeSH term(s) Animals ; Autophagosomes/metabolism ; Autophagy-Related Proteins ; Endopeptidases ; Humans ; Macroautophagy ; Membrane Proteins ; Nuclear Envelope/metabolism ; Protein Kinases ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins ; Vacuoles/metabolism ; Vesicular Transport Proteins/metabolism ; Yeasts
    Chemical Substances Autophagy-Related Proteins ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; VAC8 protein, S cerevisiae ; Vesicular Transport Proteins ; Protein Kinases (EC 2.7.-) ; ATG1 protein, S cerevisiae (EC 2.7.1.-) ; ATG21 protein, S cerevisiae (EC 3.4-) ; Endopeptidases (EC 3.4.-)
    Language English
    Publishing date 2021-12-10
    Publishing country England
    Document type Journal Article ; 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/s41467-021-27420-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Vac8 spatially confines autophagosome formation at the vacuole in

    Hollenstein, David M / Gómez-Sánchez, Rubén / Ciftci, Akif / Kriegenburg, Franziska / Mari, Muriel / Torggler, Raffaela / Licheva, Mariya / Reggiori, Fulvio / Kraft, Claudine

    Journal of cell science

    2019  Volume 132, Issue 22

    Abstract: Autophagy is initiated by the formation of a phagophore assembly site (PAS), the precursor of autophagosomes. In mammals, autophagosome formation sites form throughout the cytosol in specialized subdomains of the endoplasmic reticulum (ER). In yeast, the ...

    Abstract Autophagy is initiated by the formation of a phagophore assembly site (PAS), the precursor of autophagosomes. In mammals, autophagosome formation sites form throughout the cytosol in specialized subdomains of the endoplasmic reticulum (ER). In yeast, the PAS is also generated close to the ER, but always in the vicinity of the vacuole. How the PAS is anchored to the vacuole and the functional significance of this localization are unknown. Here, we investigated the role of the PAS-vacuole connection for bulk autophagy in the yeast
    MeSH term(s) Autophagosomes/metabolism ; Autophagy ; Membrane Proteins/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuoles/metabolism ; Vesicular Transport Proteins/metabolism
    Chemical Substances Membrane Proteins ; Saccharomyces cerevisiae Proteins ; VAC8 protein, S cerevisiae ; Vesicular Transport Proteins
    Language English
    Publishing date 2019-11-14
    Publishing country England
    Document type Journal Article ; 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.235002
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    Zs.MG 14: Show issues

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  7. Article ; Online: Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data.

    Orbán-Németh, Zsuzsanna / Beveridge, Rebecca / Hollenstein, David M / Rampler, Evelyn / Stranzl, Thomas / Hudecz, Otto / Doblmann, Johannes / Schlögelhofer, Peter / Mechtler, Karl

    Nature protocols

    2018  Volume 13, Issue 3, Page(s) 478–494

    Abstract: This protocol describes a workflow for creating structural models of proteins or protein complexes using distance restraints derived from cross-linking mass spectrometry experiments. The distance restraints are used (i) to adjust preliminary models that ... ...

    Abstract This protocol describes a workflow for creating structural models of proteins or protein complexes using distance restraints derived from cross-linking mass spectrometry experiments. The distance restraints are used (i) to adjust preliminary models that are calculated on the basis of a homologous template and primary sequence, and (ii) to select the model that is in best agreement with the experimental data. In the case of protein complexes, the cross-linking data are further used to dock the subunits to one another to generate models of the interacting proteins. Predicting models in such a manner has the potential to indicate multiple conformations and dynamic changes that occur in solution. This modeling protocol is compatible with many cross-linking workflows and uses open-source programs or programs that are free for academic users and do not require expertise in computational modeling. This protocol is an excellent additional application with which to use cross-linking results for building structural models of proteins. The established protocol is expected to take 6-12 d to complete, depending on the size of the proteins and the complexity of the cross-linking data.
    MeSH term(s) Computer Simulation ; Cross-Linking Reagents/chemistry ; Forecasting/methods ; Mass Spectrometry/methods ; Models, Molecular ; Protein Structure, Tertiary/genetics ; Protein Structure, Tertiary/physiology ; Proteins/genetics ; Proteins/physiology
    Chemical Substances Cross-Linking Reagents ; Proteins
    Language English
    Publishing date 2018-02-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2244966-8
    ISSN 1750-2799 ; 1754-2189
    ISSN (online) 1750-2799
    ISSN 1754-2189
    DOI 10.1038/nprot.2017.146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Author Correction: Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data.

    Orbán-Németh, Zsuzsanna / Beveridge, Rebecca / Hollenstein, David M / Rampler, Evelyn / Stranzl, Thomas / Hudecz, Otto / Doblmann, Johannes / Schlögelhofer, Peter / Mechtler, Karl

    Nature protocols

    2018  Volume 13, Issue 7, Page(s) 1724

    Abstract: In the version of this article initially published online, the authors used incorrectly defined restraints for specifying the distance between residues when using the HADDOCK portal. Following the publication of a Correspondence by the developers of the ... ...

    Abstract In the version of this article initially published online, the authors used incorrectly defined restraints for specifying the distance between residues when using the HADDOCK portal. Following the publication of a Correspondence by the developers of the HADDOCK portal (Nat. Protoc. https://dx.doi.org/10.1038/s41596-018-0017-6, 2018) and a Reply by the authors of the Protocol (Nat. Protoc. https://dx.doi.org/10.1038/s41596-018-0018-5, 2018), the syntax in step 21 has been corrected. In addition, the input files (available as Supplementary Data 5-7) have been replaced.
    Language English
    Publishing date 2018-06-25
    Publishing country England
    Document type Journal Article ; Published Erratum
    ZDB-ID 2244966-8
    ISSN 1750-2799 ; 1754-2189
    ISSN (online) 1750-2799
    ISSN 1754-2189
    DOI 10.1038/s41596-018-0024-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Reply to 'Defining distance restraints in HADDOCK'.

    Orbán-Németh, Zsuzsanna / Beveridge, Rebecca / Hollenstein, David M / Rampler, Evelyn / Stranzl, Thomas / Hudecz, Otto / Doblmann, Johannes / Schlögelhofer, Peter / Mechtler, Karl

    Nature protocols

    2018  Volume 13, Issue 7, Page(s) 1503–1505

    MeSH term(s) Models, Molecular ; Protein Binding
    Language English
    Publishing date 2018-06-25
    Publishing country England
    Document type Letter ; Comment
    ZDB-ID 2244966-8
    ISSN 1750-2799 ; 1754-2189
    ISSN (online) 1750-2799
    ISSN 1754-2189
    DOI 10.1038/s41596-018-0018-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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