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  1. Article ; Online: Autophagy.

    Wollert, Thomas

    Current biology : CB

    2019  Volume 29, Issue 14, Page(s) R671–R677

    Abstract: In 1955, the biologist and Nobel Prize laureate Christian de Duve discovered that cells possess specialized organelles filled with hydrolytic enzymes and he called these organelles lysosomes. At the same time, electron microscopy studies by Novikoff and ... ...

    Abstract In 1955, the biologist and Nobel Prize laureate Christian de Duve discovered that cells possess specialized organelles filled with hydrolytic enzymes and he called these organelles lysosomes. At the same time, electron microscopy studies by Novikoff and colleagues showed that intracellular dense bodies, which later turned out to be lysosomes, contain cytoplasmic components. Together, these groundbreaking observations revealed that cells can deliver cytoplasmic components to lysosomes for degradation. The hallmark of this degradative process, which de Duve called autophagy, is the formation of double-membrane-limited vesicles. Further morphological characterization of these vesicles (autophagosomes) revealed that they mainly contain bulk cytoplasm. Although this suggested that autophagy leads to a non-selective degradation of cytoplasmic material, de Duve anticipated that a regulated and selective type of this pathway must also exist. Today we know that, under normal conditions, macroautophagy is a highly selective pathway that sequesters damaged or superfluous material from the cytoplasm through the formation of double-membrane-limited autophagosomes. Upon fusion with lysosomes, the content of autophagosomes is degraded and the resulting building blocks are released into the cytoplasm. However, in response to cytotoxic stress or starvation, cells start to produce autophagosomes that capture bulk cytoplasm non-selectively. This stress response is essential for cells to survive adverse environmental conditions, whereas the selective sequestration of cargo is important to maintain cellular homeostasis.
    MeSH term(s) Autophagosomes/metabolism ; Autophagy/physiology ; Cytosol/metabolism ; Lysosomes/metabolism ; Macroautophagy/physiology
    Language English
    Publishing date 2019-08-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2019.06.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Don't forget to be picky - selective autophagy of protein aggregates in neurodegenerative diseases.

    Simonsen, Anne / Wollert, Thomas

    Current opinion in cell biology

    2022  Volume 75, Page(s) 102064

    Abstract: The homeostasis of cells depends on the selective degradation of damaged or superfluous cellular components. Autophagy is the major pathway that recognizes such components, sequesters them in de novo formed autophagosomes and delivers them to lysosomes ... ...

    Abstract The homeostasis of cells depends on the selective degradation of damaged or superfluous cellular components. Autophagy is the major pathway that recognizes such components, sequesters them in de novo formed autophagosomes and delivers them to lysosomes for degradation. The recognition of specific cargo and the biogenesis of autophagosomes involve a dedicated machinery of autophagy related (ATG) proteins. Intense research over the past decades has revealed insights into the function of autophagy proteins and mechanisms that govern cargo recognition. Other aspects including the molecular mechanisms involved in the onset of human diseases are less well understood. However, autophagic dysfunctions, caused by age related decline in autophagy or mutations in ATG proteins, are directly related to a large number of human pathologies including neurodegenerative disorders. Here, we review most recent discoveries and breakthroughs in selective autophagy and its relationship to neurodegeneration.
    MeSH term(s) Autophagosomes ; Autophagy ; Humans ; Lysosomes ; Neurodegenerative Diseases ; Protein Aggregates
    Chemical Substances Protein Aggregates
    Language English
    Publishing date 2022-02-28
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2022.01.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Membrane remodeling by SARS-CoV-2 - double-enveloped viral replication.

    Mohan, Jagan / Wollert, Thomas

    Faculty reviews

    2021  Volume 10, Page(s) 17

    Abstract: The ongoing pandemic of the new severe acute respiratory syndrome coronavirus (SARS-CoV-2) has caused more than one million deaths, overwhelmed many public health systems, and led to a worldwide economic recession. This has raised an unprecedented need ... ...

    Abstract The ongoing pandemic of the new severe acute respiratory syndrome coronavirus (SARS-CoV-2) has caused more than one million deaths, overwhelmed many public health systems, and led to a worldwide economic recession. This has raised an unprecedented need to develop antiviral drugs and vaccines, which requires profound knowledge of the fundamental pathology of the virus, including its entry, replication, and release from host cells. The genome of coronaviruses comprises around 30 kb of positive single-stranded RNA, representing one of the largest RNA genomes of viruses. The 5' part of the genome encodes a large polyprotein, PP1ab, which gives rise to 16 non-structural proteins (nsp1- nsp16). Two proteases encoded in nsp3 and nsp5 cleave the polyprotein into individual proteins. Most nsps belong to the viral replicase complex that promotes replication of the viral genome and translation of structural proteins by producing subgenomic mRNAs. The replicase complexes are found on double-membrane vesicles (DMVs) that contain viral double-stranded RNA. Expression of a small subset of viral proteins, including nsp3 and nsp4, is sufficient to induce formation of these DMVs in human cells, suggesting that both proteins deform host membranes into such structures. We will discuss the formation of DMVs and provide an overview of other membrane remodeling processes that are induced by coronaviruses.
    Language English
    Publishing date 2021-02-22
    Publishing country England
    Document type Journal Article ; Review
    ISSN 2732-432X
    ISSN (online) 2732-432X
    DOI 10.12703/r/10-17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Reconstituting multivesicular body biogenesis with purified components.

    Wollert, Thomas

    Methods in cell biology

    2012  Volume 108, Page(s) 73–92

    Abstract: Activated cell surface receptors are rapidly removed from the plasma membrane through clathrin mediated endocytosis and transported to the endosome where they are either recycled or sorted to the lysosomal pathway to be degraded. Receptors, destined for ... ...

    Abstract Activated cell surface receptors are rapidly removed from the plasma membrane through clathrin mediated endocytosis and transported to the endosome where they are either recycled or sorted to the lysosomal pathway to be degraded. Receptors, destined for degradation in the lysosome, are packaged into intraluminal vesicles (ILVs) of endosomes by a reaction that is topologically unrelated to other budding reactions in cells. First, receptors are clustered at the endosomal membrane and receptor-rich membrane patches then bud towards the lumen of the endosome. The nascent membrane buds are finally cleaved from the limiting membrane to release cargo-bearing vesicles into the endosomal interior. The molecular machinery that drives multivesicular body biogenesis, the endosomal sorting complex required for transport (ESCRT) machinery, has been identified through genetic screens. It consists of the cytoplasmic, hetero-multimeric complexes ESCRT-0, -I, -II, and -III, and of the Vps4/VtaI complex. Although the ESCRT machinery has been characterized extensively using cell-biological and biochemical approaches, the molecular mechanism of multivesicular body biogenesis remained unclear. In this chapter, I will present in vitro reconstitution systems that we used to study ESCRT-driven membrane remodeling reactions with purified components on artificial membranes. This includes generation of large and giant unilamellar liposomes, as well as in vitro reconstitution reactions of fluorescently labeled proteins on such membranes. I will discuss both, the potential of in vitro systems to analyze membrane-remodeling events and also their limitations.
    MeSH term(s) Algorithms ; Animals ; Biological Transport ; Endosomal Sorting Complexes Required for Transport/chemistry ; Fluorescence Recovery After Photobleaching ; Humans ; Membrane Lipids/chemistry ; Membrane Proteins/chemistry ; Models, Biological ; Multivesicular Bodies/chemistry ; Protein Binding ; Unilamellar Liposomes/chemistry
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Membrane Lipids ; Membrane Proteins ; Unilamellar Liposomes
    Language English
    Publishing date 2012
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ISSN 0091-679X
    ISSN 0091-679X
    DOI 10.1016/B978-0-12-386487-1.00004-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Reconstituting Autophagy Initiation from Purified Components.

    Mayrhofer, Peter / Wollert, Thomas

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

    2018  Volume 1880, Page(s) 119–133

    Abstract: The hallmark of macroautophagy is the de novo generation of a membrane structure that collects cytoplasmic material and delivers it to lysosomes for degradation. The nucleation of this precursor membrane, termed phagophore, involves the coordinated ... ...

    Abstract The hallmark of macroautophagy is the de novo generation of a membrane structure that collects cytoplasmic material and delivers it to lysosomes for degradation. The nucleation of this precursor membrane, termed phagophore, involves the coordinated assembly of the Atg1-kinase complex and the recruitment of Atg9 vesicles. The latter represents one important membrane source in order to produce phagophores in vivo. We explain how the process of phagophore nucleation can be reconstituted from purified components in vitro. We describe the assembly of the ~500 kDa pentameric Atg1-kinase complex from its purified subunits. We also explain how Atg9-donor vesicles are generated in vitro to study the interaction of Atg9 and Atg1-kinase complexes by floatation experiments.
    MeSH term(s) Animals ; Autophagy ; Autophagy-Related Proteins/chemistry ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/isolation & purification ; Autophagy-Related Proteins/metabolism ; Chromatography, Affinity/methods ; Chromatography, Gel/methods ; Cloning, Molecular/methods ; Escherichia coli/genetics ; Humans ; Liposomes/chemistry ; Liposomes/metabolism ; Protein Multimerization
    Chemical Substances Autophagy-Related Proteins ; Liposomes
    Language English
    Publishing date 2018-12-20
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-8873-0_6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Reconstruction of destruction -

    Moparthi, Satish Babu / Wollert, Thomas

    Journal of cell science

    2018  Volume 132, Issue 4

    Abstract: Autophagy is one of the most elaborative membrane remodeling systems in eukaryotic cells. Its major function is to recycle cytoplasmic material by delivering it to lysosomes for degradation. To achieve this, a membrane cisterna is formed that gradually ... ...

    Abstract Autophagy is one of the most elaborative membrane remodeling systems in eukaryotic cells. Its major function is to recycle cytoplasmic material by delivering it to lysosomes for degradation. To achieve this, a membrane cisterna is formed that gradually captures cargo such as organelles or protein aggregates. The diversity of cargo requires autophagy to be highly versatile to adapt the shape of the phagophore to its substrate. Upon closure of the phagophore, a double-membrane-surrounded autophagosome is formed that eventually fuses with lysosomes. In response to environmental cues such as cytotoxicity or starvation, bulk cytoplasm can be captured and delivered to lysosomes. Autophagy thus supports cellular survival under adverse conditions. During the past decades, groundbreaking genetic and cell biological studies have identified the core machinery involved in the process. In this Review, we are focusing on
    MeSH term(s) Animals ; Autophagosomes/metabolism ; Autophagy/physiology ; Humans ; Lysosomes/metabolism ; Membranes/metabolism ; Phagosomes/metabolism ; Proteins/metabolism
    Chemical Substances Proteins
    Language English
    Publishing date 2018-10-31
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.223792
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Human ubiquitin-like proteins as central coordinators in autophagy.

    Mohan, Jagan / Wollert, Thomas

    Interface focus

    2018  Volume 8, Issue 5, Page(s) 20180025

    Abstract: Autophagy is one of the most versatile recycling systems of eukaryotic cells. It degrades diverse cytoplasmic components such as organelles, protein aggregates, ribosomes and multi-enzyme complexes. Not surprisingly, any failure of autophagy or reduced ... ...

    Abstract Autophagy is one of the most versatile recycling systems of eukaryotic cells. It degrades diverse cytoplasmic components such as organelles, protein aggregates, ribosomes and multi-enzyme complexes. Not surprisingly, any failure of autophagy or reduced activity of the pathway contributes to the onset of various pathologies, including neurodegeneration, cancer and metabolic disorders such as diabetes or immune diseases. Furthermore, autophagy contributes to the innate immune response and combats bacterial or viral pathogens. The hallmark of macroautophagy is the formation of a membrane sack that sequesters cytoplasmic cargo and delivers it to lysosomes for degradation. More than 40 autophagy-related (ATG) proteins have so far been identified. A unique protein-conjugation system represents one of the core components of this highly elaborate machinery. It conjugates six homologous ATG8 family proteins to the autophagic membrane. In this review, we summarize the current knowledge regarding the various functions of ATG8 proteins in autophagy and briefly discuss how physical approaches and
    Language English
    Publishing date 2018-08-17
    Publishing country England
    Document type Journal Article
    ISSN 2042-8898
    ISSN 2042-8898
    DOI 10.1098/rsfs.2018.0025
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  8. Article ; Online: Digesting cytotoxic stressors - an unconventional mechanism to induce autophagy.

    Langlois, Christine R / Wollert, Thomas

    The FEBS journal

    2016  Volume 283, Issue 21, Page(s) 3886–3888

    Abstract: Autophagy is an essential and fundamental pathway that clears unwanted or damaged material from the cell. Initiation of autophagy was previously shown to be dependent on the Ulk1/2 kinase complex. In this issue of The FEBS Journal, Braden and Neufeld ... ...

    Abstract Autophagy is an essential and fundamental pathway that clears unwanted or damaged material from the cell. Initiation of autophagy was previously shown to be dependent on the Ulk1/2 kinase complex. In this issue of The FEBS Journal, Braden and Neufeld investigated the Ulk3 homolog in Drosophila, and proposed a novel, Ulk1/2 independent pathway for autophagy initiation.
    MeSH term(s) Autophagy
    Language English
    Publishing date 2016
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13919
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  9. Book ; Online ; Thesis: Rational pathogen design

    Wollert, Thomas

    extending the host range of Listeria monocytogenes by thermodynamically re-engineering the internalin, E-cadherin interface

    2007  

    Author's details von Thomas Wollert
    Language English
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Techn. Univ., Diss--Braunschweig, 2007
    Database Former special subject collection: coastal and deep sea fishing

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  10. Article ; Online: Cell scientist to watch - Thomas Wollert.

    Wollert, Thomas / Bobrowska, Anna

    Journal of cell science

    2015  Volume 128, Issue 20, Page(s) 3685–3686

    Abstract: Thomas Wollert pursued his PhD in the laboratories of Wolf-Dieter Schubert and Dirk Heinz at the Helmholtz Centre for Infection Research in Braunschweig, Germany. In 2008, he moved to the USA for a postdoctoral position with James Hurley at the National ... ...

    Abstract Thomas Wollert pursued his PhD in the laboratories of Wolf-Dieter Schubert and Dirk Heinz at the Helmholtz Centre for Infection Research in Braunschweig, Germany. In 2008, he moved to the USA for a postdoctoral position with James Hurley at the National Institutes of Health in Bethesda, MD, as an EMBO Long Term Fellow. In 2010, Thomas returned to Germany to start his own group at the Max Planck Institute of Biochemistry in Martinsried. His work has been recognised with awards from the German Society for Molecular Biology and Biochemistry, and the German Genetics Society. More recently, Thomas received the 2014 Walter Flemming Medal from the German Society for Cell Biology, the 2015 EMBO Young Investigator Award and the 2015 Eppendorf Prize for Young European Investigators. His laboratory combines biophysics with cell biology in order to study the process of autophagosome formation.
    MeSH term(s) Animals ; Biophysics/history ; Cell Biology/history ; History, 21st Century ; Humans ; Portraits as Topic
    Language English
    Publishing date 2015-10-15
    Publishing country England
    Document type Historical Article ; Interview
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.179069
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