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  1. Article ; Online: The Role of ATG9 Vesicles in Autophagosome Biogenesis.

    Holzer, Elisabeth / Martens, Sascha / Tulli, Susanna

    Journal of molecular biology

    2024  , Page(s) 168489

    Abstract: Autophagy mediates the degradation and recycling of cellular material in the lysosomal system. Dysfunctional autophagy is associated with a plethora of diseases including uncontrolled infections, cancer and neurodegeneration. In macroautophagy (hereafter ...

    Abstract Autophagy mediates the degradation and recycling of cellular material in the lysosomal system. Dysfunctional autophagy is associated with a plethora of diseases including uncontrolled infections, cancer and neurodegeneration. In macroautophagy (hereafter autophagy) this material is encapsulated in double membrane vesicles, the autophagosomes, which form upon induction of autophagy. The precursors to autophagosomes, referred to as phagophores, first appear as small flattened membrane cisternae, which gradually enclose the cargo material as they grow. The assembly of phagophores during autophagy initiation has been a major subject of investigation over the past decades. A special focus has been ATG9, the only conserved transmembrane protein among the core machinery. The majority of ATG9 localizes to small Golgi-derived vesicles. Here we review the recent advances and breakthroughs regarding our understanding of how ATG9 and the vesicles it resides in serve to assemble the autophagy machinery and to establish membrane contact sites for autophagosome biogenesis. We also highlight open questions in the field that need to be addressed in the years to come.
    Language English
    Publishing date 2024-02-10
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2024.168489
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  2. Article ; Online: A division of labor in mTORC1 signaling and autophagy.

    Martens, Sascha

    Science signaling

    2018  Volume 11, Issue 559

    Abstract: In human cells, the p62 protein acts as an adaptor in various signaling pathways as well as a receptor for selective autophagy. In this issue ... ...

    Abstract In human cells, the p62 protein acts as an adaptor in various signaling pathways as well as a receptor for selective autophagy. In this issue of
    MeSH term(s) Adaptor Proteins, Signal Transducing ; Autophagy ; Humans ; Mechanistic Target of Rapamycin Complex 1 ; Nutrients ; Proteolysis ; Sequestosome-1 Protein
    Chemical Substances Adaptor Proteins, Signal Transducing ; Nutrients ; SQSTM1 protein, human ; Sequestosome-1 Protein ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
    Language English
    Publishing date 2018-12-04
    Publishing country United States
    Document type Journal Article ; Review ; Comment
    ZDB-ID 2417226-1
    ISSN 1937-9145 ; 1945-0877
    ISSN (online) 1937-9145
    ISSN 1945-0877
    DOI 10.1126/scisignal.aav3530
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The membrane surface as a platform that organizes cellular and biochemical processes.

    Leonard, Thomas A / Loose, Martin / Martens, Sascha

    Developmental cell

    2023  Volume 58, Issue 15, Page(s) 1315–1332

    Abstract: Membranes are essential for life. They act as semi-permeable boundaries that define cells and organelles. In addition, their surfaces actively participate in biochemical reaction networks, where they confine proteins, align reaction partners, and ... ...

    Abstract Membranes are essential for life. They act as semi-permeable boundaries that define cells and organelles. In addition, their surfaces actively participate in biochemical reaction networks, where they confine proteins, align reaction partners, and directly control enzymatic activities. Membrane-localized reactions shape cellular membranes, define the identity of organelles, compartmentalize biochemical processes, and can even be the source of signaling gradients that originate at the plasma membrane and reach into the cytoplasm and nucleus. The membrane surface is, therefore, an essential platform upon which myriad cellular processes are scaffolded. In this review, we summarize our current understanding of the biophysics and biochemistry of membrane-localized reactions with particular focus on insights derived from reconstituted and cellular systems. We discuss how the interplay of cellular factors results in their self-organization, condensation, assembly, and activity, and the emergent properties derived from them.
    MeSH term(s) Cell Membrane/metabolism ; Membranes ; Signal Transduction ; Cell Nucleus
    Language English
    Publishing date 2023-07-06
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2023.06.001
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  4. Article ; Online: Aggrephagy at a glance.

    Bauer, Bernd / Martens, Sascha / Ferrari, Luca

    Journal of cell science

    2023  Volume 136, Issue 10

    Abstract: Cells keep their proteome functional by the action of the proteostasis network, composed of the chaperones, the ubiquitin-proteasome system and autophagy. The decline of this network results in the accumulation of protein aggregates and is associated ... ...

    Abstract Cells keep their proteome functional by the action of the proteostasis network, composed of the chaperones, the ubiquitin-proteasome system and autophagy. The decline of this network results in the accumulation of protein aggregates and is associated with aging and disease. In this Cell Science at a Glance and accompanying poster, we provide an overview of the molecular mechanisms of the removal of protein aggregates by a selective autophagy pathway, termed aggrephagy. We outline how aggrephagy is regulated by post-translational modifications and via auxiliary proteins. We further describe alternative aggrephagy pathways in physiology and their disruption in pathology. In particular, we discuss aggrephagy pathways in neurons and accumulation of protein aggregates in a wide range of diseases. Finally, we highlight strategies to reprogram aggrephagy to treat protein aggregation diseases.
    MeSH term(s) Autophagy ; Macroautophagy ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Protein Aggregates ; Proteostasis ; Humans
    Chemical Substances Molecular Chaperones ; Protein Aggregates
    Language English
    Publishing date 2023-05-31
    Publishing country England
    Document type Journal Article ; Review ; 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.260888
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  5. Article ; Online: Sequestration of translation initiation factors in p62 condensates

    Alberto Danieli / Georg Vucak / Manuela Baccarini / Sascha Martens

    Cell Reports, Vol 42, Iss 12, Pp 113583- (2023)

    2023  

    Abstract: Summary: Selective autophagy mediates the removal of harmful material from the cytoplasm. This cargo material is selected by cargo receptors, which orchestrate its sequestration within double-membrane autophagosomes and subsequent lysosomal degradation. ... ...

    Abstract Summary: Selective autophagy mediates the removal of harmful material from the cytoplasm. This cargo material is selected by cargo receptors, which orchestrate its sequestration within double-membrane autophagosomes and subsequent lysosomal degradation. The cargo receptor p62/SQSTM1 is present in cytoplasmic condensates, and a fraction of them are constantly delivered into lysosomes. However, the molecular composition of the p62 condensates is incompletely understood. To obtain insights into their composition, we develop a method to isolate these condensates and find that p62 condensates are enriched in components of the translation machinery. Furthermore, p62 interacts with translation initiation factors, and eukaryotic initiation factor 2α (eIF2α) and eIF4E are degraded by autophagy in a p62-dependent manner. Thus, p62-mediated autophagy may in part be linked to down-regulation of translation initiation. The p62 condensate isolation protocol developed here may facilitate the study of their contribution to cellular quality control and their roles in health and disease.
    Keywords CP: Cell biology ; CP: Molecular biology ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: p62 and NBR1 functions are dispensable for aggrephagy in mouse ESCs and ESC-derived neurons.

    Trapannone, Riccardo / Romanov, Julia / Martens, Sascha

    Life science alliance

    2023  Volume 6, Issue 11

    Abstract: Accumulation of protein aggregates is a hallmark of various neurodegenerative diseases. Selective autophagy mediates the delivery of specific cytoplasmic cargo material into lysosomes for degradation. In aggrephagy, which is the selective autophagy of ... ...

    Abstract Accumulation of protein aggregates is a hallmark of various neurodegenerative diseases. Selective autophagy mediates the delivery of specific cytoplasmic cargo material into lysosomes for degradation. In aggrephagy, which is the selective autophagy of protein aggregates, the cargo receptors p62 and NBR1 were shown to play important roles in cargo selection. They bind ubiquitinated cargo material via their ubiquitin-associated domains and tether it to autophagic membranes via their LC3-interacting regions. We used mouse embryonic stem cells (ESCs) in combination with genome editing to obtain further insights into the roles of p62 and NBR1 in aggrephagy. Unexpectedly, our data reveal that both ESCs and ESC-derived neurons do not show strong defects in the clearance of protein aggregates upon knockout of p62 or NBR1 and upon mutation of the p62 ubiquitin-associated domain and the LC3-interacting region motif. Taken together, our results show a robust aggregate clearance in ESCs and ESC-derived neurons. Thus, redundancy between the cargo receptors, other factors, and pathways, such as the ubiquitin-proteasome system, may compensate for the loss of function of p62 and NBR1.
    MeSH term(s) Animals ; Mice ; Lysosomes ; Macroautophagy ; Mouse Embryonic Stem Cells ; Neurons ; Protein Aggregates ; Ubiquitins ; Nuclear Pore Complex Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism
    Chemical Substances Protein Aggregates ; Ubiquitins ; NUP62 protein, mouse ; Nbr1 protein, mouse ; Nuclear Pore Complex Proteins ; Intracellular Signaling Peptides and Proteins
    Language English
    Publishing date 2023-08-24
    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.202301936
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  7. Article ; Online: Sequestration of translation initiation factors in p62 condensates.

    Danieli, Alberto / Vucak, Georg / Baccarini, Manuela / Martens, Sascha

    Cell reports

    2023  Volume 42, Issue 12, Page(s) 113583

    Abstract: Selective autophagy mediates the removal of harmful material from the cytoplasm. This cargo material is selected by cargo receptors, which orchestrate its sequestration within double-membrane autophagosomes and subsequent lysosomal degradation. The cargo ...

    Abstract Selective autophagy mediates the removal of harmful material from the cytoplasm. This cargo material is selected by cargo receptors, which orchestrate its sequestration within double-membrane autophagosomes and subsequent lysosomal degradation. The cargo receptor p62/SQSTM1 is present in cytoplasmic condensates, and a fraction of them are constantly delivered into lysosomes. However, the molecular composition of the p62 condensates is incompletely understood. To obtain insights into their composition, we develop a method to isolate these condensates and find that p62 condensates are enriched in components of the translation machinery. Furthermore, p62 interacts with translation initiation factors, and eukaryotic initiation factor 2α (eIF2α) and eIF4E are degraded by autophagy in a p62-dependent manner. Thus, p62-mediated autophagy may in part be linked to down-regulation of translation initiation. The p62 condensate isolation protocol developed here may facilitate the study of their contribution to cellular quality control and their roles in health and disease.
    MeSH term(s) Humans ; HEK293 Cells ; RNA-Binding Proteins/metabolism ; Biomolecular Condensates/drug effects ; Biomolecular Condensates/metabolism ; Eukaryotic Initiation Factor-2/antagonists & inhibitors ; Eukaryotic Initiation Factor-2/metabolism ; Eukaryotic Initiation Factor-4E/antagonists & inhibitors ; Eukaryotic Initiation Factor-4E/metabolism ; Autophagy/drug effects ; Autophagy/genetics ; Wortmannin/pharmacology
    Chemical Substances P62 protein, human ; RNA-Binding Proteins ; Eukaryotic Initiation Factor-2 ; Eukaryotic Initiation Factor-4E ; Wortmannin (XVA4O219QW)
    Language English
    Publishing date 2023-12-12
    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.2023.113583
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  8. Article ; Online: Faa1 membrane binding drives positive feedback in autophagosome biogenesis via fatty acid activation.

    Baumann, Verena / Achleitner, Sonja / Tulli, Susanna / Schuschnig, Martina / Klune, Lara / Martens, Sascha

    The Journal of cell biology

    2024  Volume 223, Issue 7

    Abstract: Autophagy serves as a stress response pathway by mediating the degradation of cellular material within lysosomes. In autophagy, this material is encapsulated in double-membrane vesicles termed autophagosomes, which form from precursors referred to as ... ...

    Abstract Autophagy serves as a stress response pathway by mediating the degradation of cellular material within lysosomes. In autophagy, this material is encapsulated in double-membrane vesicles termed autophagosomes, which form from precursors referred to as phagophores. Phagophores grow by lipid influx from the endoplasmic reticulum into Atg9-positive compartments and local lipid synthesis provides lipids for their expansion. How phagophore nucleation and expansion are coordinated with lipid synthesis is unclear. Here, we show that Faa1, an enzyme activating fatty acids, is recruited to Atg9 vesicles by directly binding to negatively charged membranes with a preference for phosphoinositides such as PI3P and PI4P. We define the membrane-binding surface of Faa1 and show that its direct interaction with the membrane is required for its recruitment to phagophores. Furthermore, the physiological localization of Faa1 is key for its efficient catalysis and promotes phagophore expansion. Our results suggest a positive feedback loop coupling phagophore nucleation and expansion to lipid synthesis.
    MeSH term(s) Autophagosomes ; Autophagy ; Fatty Acids/metabolism ; Feedback ; Macroautophagy ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Fatty Acids ; Faa1 protein, S cerevisiae (EC 6.2.1.-)
    Language English
    Publishing date 2024-04-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202309057
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  9. Article ; Online: Necessary, but also Sufficient?

    Martens, Sascha

    Trends in cell biology

    2016  Volume 26, Issue 7, Page(s) 467–469

    Abstract: Cell biologists are equipped with a plethora of techniques and approaches to unravel the fascinating inner working of the cell. Among these, biochemistry has the ability to define the machinery that is both necessary and sufficient for a given process ... ...

    Abstract Cell biologists are equipped with a plethora of techniques and approaches to unravel the fascinating inner working of the cell. Among these, biochemistry has the ability to define the machinery that is both necessary and sufficient for a given process and, therefore, to define its core mechanism.
    Language English
    Publishing date 2016-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2016.04.004
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  10. Article ; Online: No ATG8s, no problem? How LC3/GABARAP proteins contribute to autophagy.

    Martens, Sascha

    The Journal of cell biology

    2016  Volume 215, Issue 6, Page(s) 761–763

    Abstract: The ATG8 family LC3/GABARAP proteins are attached to the membrane of nascent autophagosomes, but their functions during autophagy are unclear. In this issue, Nguyen et al. (2016. J. Cell Biol. https://doi.org/10.1083/jcb.201607039) show that LC3/GABARAP ... ...

    Abstract The ATG8 family LC3/GABARAP proteins are attached to the membrane of nascent autophagosomes, but their functions during autophagy are unclear. In this issue, Nguyen et al. (2016. J. Cell Biol. https://doi.org/10.1083/jcb.201607039) show that LC3/GABARAP proteins are not essential for autophagosome formation but are critical for autophagosome-lysosome fusion.
    MeSH term(s) Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Autophagy ; Autophagy-Related Protein 8 Family/metabolism ; HeLa Cells ; Humans ; Microtubule-Associated Proteins/metabolism ; Mitochondria/metabolism ; Models, Biological ; Phagosomes/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Autophagy-Related Protein 8 Family ; Microtubule-Associated Proteins
    Language English
    Publishing date 2016-12-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201611116
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