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  1. Article ; Online: Tether Me, Tether Me Not-Dynamic Organelle Contact Sites in Metabolic Rewiring.

    Bohnert, Maria

    Developmental cell

    2020  Volume 54, Issue 2, Page(s) 212–225

    Abstract: Membrane contact sites (CSs) are specialized cellular regions where distinct organelles are actively positioned very close to each other, at a distance of just a few nanometers. Structurally, CS formation depends on tether proteins that physically link ... ...

    Abstract Membrane contact sites (CSs) are specialized cellular regions where distinct organelles are actively positioned very close to each other, at a distance of just a few nanometers. Structurally, CS formation depends on tether proteins that physically link organellar membranes to each other. Functionally, these structures act as hotspots for communication and material transfer. In recent years, we are starting to understand that the cellular CS landscape is not static but instead responds dynamically to diverse metabolic cues. This review describes the interplay between cellular metabolism and CS-based organelle communication and discusses molecular mechanisms of contact modulation in cellular adaptation to changing metabolic requirements.
    MeSH term(s) Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Organelles/metabolism ; Saccharomyces cerevisiae/metabolism
    Language English
    Publishing date 2020-07-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2020.06.026
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  2. Article ; Online: New friends for seipin - Implications of seipin partner proteins in the life cycle of lipid droplets.

    Bohnert, Maria

    Seminars in cell & developmental biology

    2020  Volume 108, Page(s) 24–32

    Abstract: Lipids act as building blocks for all cellular membranes and as key energy carriers. Neutral storage lipids are packaged into specialized organelles termed Lipid Droplets (LDs). LDs dynamically respond to the metabolic state of the cell, and undergo ... ...

    Abstract Lipids act as building blocks for all cellular membranes and as key energy carriers. Neutral storage lipids are packaged into specialized organelles termed Lipid Droplets (LDs). LDs dynamically respond to the metabolic state of the cell, and undergo cycles of de novo biogenesis, growth, shrinkage, and consumption. How these processes are mediated on a molecular level is a key objective of the LD field. The yeast Lipid Droplet Organization (LDO) proteins and the human promethin/TMEM159/LDAF1 are newly identified molecular players involved in different aspects of the life cycle of LDs. These factors show remote homology to each other, and are physically and functionally linked to seipin, a central component in LD formation and adipogenesis.
    MeSH term(s) Animals ; Autophagy ; Humans ; Lipid Droplets/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Models, Biological ; Proteome/metabolism
    Chemical Substances Membrane Proteins ; Proteome
    Language English
    Publishing date 2020-05-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2020.04.012
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  3. Article ; Online: Hard to handle: how lipid saturation affects the nuclear envelope.

    Höhne, Pascal / Bohnert, Maria

    Trends in cell biology

    2023  Volume 34, Issue 1, Page(s) 1–2

    Abstract: The nuclear envelope is a unique subdomain of the endoplasmic reticulum (ER) that encapsulates the genome and mediates communication between the nucleus and the rest of the cell via nuclear pore complexes. A recent study by Romanauska and Köhler shows ... ...

    Abstract The nuclear envelope is a unique subdomain of the endoplasmic reticulum (ER) that encapsulates the genome and mediates communication between the nucleus and the rest of the cell via nuclear pore complexes. A recent study by Romanauska and Köhler shows that balanced lipid unsaturation is critical for nuclear envelope and nuclear pore complex architecture and function.
    MeSH term(s) Humans ; Nuclear Envelope ; Nuclear Pore ; Endoplasmic Reticulum ; Lipids
    Chemical Substances Lipids
    Language English
    Publishing date 2023-11-08
    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.2023.10.011
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  4. Article ; Online: Organelle Contact Sites: Lipid Droplets Hooked by Metabolically Controlled Tethers.

    Bohnert, Maria

    Current biology : CB

    2019  Volume 29, Issue 10, Page(s) R375–R377

    Abstract: Lipid droplets are physically linked to other organelles via contact sites for communication, but the underlying molecular machineries are poorly characterized. Recent studies identify metabolically controlled sorting nexin tether proteins as important ... ...

    Abstract Lipid droplets are physically linked to other organelles via contact sites for communication, but the underlying molecular machineries are poorly characterized. Recent studies identify metabolically controlled sorting nexin tether proteins as important players at these sites.
    MeSH term(s) Cerebellar Ataxia ; Humans ; Lipid Droplets ; Mitochondrial Membranes ; Organelles ; Protein Transport
    Language English
    Publishing date 2019-04-23
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2019.03.049
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  5. Article ; Online: Tethering Fat

    Maria Bohnert

    Contact, Vol

    Tethers in Lipid Droplet Contact Sites

    2020  Volume 3

    Abstract: Lipid droplets (LDs) are central hubs in cellular lipid handling. They serve as lipid storage organelles and are involved in neutral lipid biosynthesis and breakdown as well as in the production of phospholipids and sterols. For communication with other ... ...

    Abstract Lipid droplets (LDs) are central hubs in cellular lipid handling. They serve as lipid storage organelles and are involved in neutral lipid biosynthesis and breakdown as well as in the production of phospholipids and sterols. For communication with other organelles, LDs are heavily engaged in contact sites. The molecular basis of these structures is formed by proteins or protein complexes termed tethers, which attach partner organelles to the surface of LDs. Here, we describe the structural and functional characteristics of recently identified LD tethers. Intriguingly, these LD tethers have additional features, such as the structural capacity to form tri-organellar contacts, domains specialized for interorganellar bulk lipid transfer, and connections to specific lipid metabolism enzymes, which might collectively contribute to the key role of LDs in cellular lipid flux.
    Keywords Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
    Language English
    Publishing date 2020-03-01T00:00:00Z
    Publisher SAGE Publishing
    Document type Article ; Online
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  6. Article ; Online: Wrapping up the fats-a structure of the lipid droplet biogenesis protein seipin.

    Bohnert, Maria

    The Journal of cell biology

    2018  Volume 217, Issue 12, Page(s) 4053–4054

    Abstract: The lipid droplet (LD) biogenesis protein seipin is crucial for formation of normal LDs, but its exact functional role has been enigmatic. In this issue, Sui et al. (2018. ...

    Abstract The lipid droplet (LD) biogenesis protein seipin is crucial for formation of normal LDs, but its exact functional role has been enigmatic. In this issue, Sui et al. (2018.
    MeSH term(s) Cryoelectron Microscopy ; GTP-Binding Protein gamma Subunits ; Lipid Droplets ; Membrane Proteins ; Saccharomyces cerevisiae Proteins
    Chemical Substances GTP-Binding Protein gamma Subunits ; Membrane Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2018-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201811021
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  7. Article ; Online: A move in response to starvation.

    Fausten, Rebecca Martina / Bohnert, Maria

    eLife

    2021  Volume 10

    Abstract: When a yeast cell runs out of fuel, it can increase the flux through a central metabolic pathway by simply changing the location of an enzyme. ...

    Abstract When a yeast cell runs out of fuel, it can increase the flux through a central metabolic pathway by simply changing the location of an enzyme.
    MeSH term(s) Humans ; Hydroxymethylglutaryl CoA Reductases/metabolism ; Metabolic Networks and Pathways ; Mevalonic Acid ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Starvation
    Chemical Substances Hydroxymethylglutaryl CoA Reductases (EC 1.1.1.-) ; Mevalonic Acid (S5UOB36OCZ)
    Language English
    Publishing date 2021-06-01
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.69680
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  8. Article ; Online: The Sweet and Sour Taste of Phosphoinositide Signaling: Protonation of PI4P Modulates Its Function in Response to Cytoplasmic pH Changes.

    Schmidt, Oliver / Bohnert, Maria

    Developmental cell

    2020  Volume 52, Issue 4, Page(s) 395–397

    Abstract: Phosphoinositides are signaling lipids that recruit effector proteins to membranes. Shin et al. show that a glucose-starvation-induced drop in cytosolic pH alters the protonation state of the phosphoinositide PI4P, resulting in dissociation of its ... ...

    Abstract Phosphoinositides are signaling lipids that recruit effector proteins to membranes. Shin et al. show that a glucose-starvation-induced drop in cytosolic pH alters the protonation state of the phosphoinositide PI4P, resulting in dissociation of its effector Osh1 from the trans-Golgi network membrane and metabolic regulation of lipid and protein sorting.
    MeSH term(s) Hydrogen-Ion Concentration ; Phosphatidylinositol Phosphates ; Phosphatidylinositols ; Protein Transport ; Taste
    Chemical Substances Phosphatidylinositol Phosphates ; Phosphatidylinositols
    Language English
    Publishing date 2020-02-24
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2020.01.035
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  9. Article ; Online: A move in response to starvation

    Rebecca Martina Fausten / Maria Bohnert

    eLife, Vol

    2021  Volume 10

    Abstract: When a yeast cell runs out of fuel, it can increase the flux through a central metabolic pathway by simply changing the location of an enzyme. ...

    Abstract When a yeast cell runs out of fuel, it can increase the flux through a central metabolic pathway by simply changing the location of an enzyme.
    Keywords lipid droplet ; mevalonate ; nucleus-vacuole junction ; sterol-ester ; HMG-CoA Reductase ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
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  10. Article ; Online: Born this way - Biogenesis of lipid droplets from specialized ER subdomains.

    Nettebrock, Niclas T / Bohnert, Maria

    Biochimica et biophysica acta. Molecular and cell biology of lipids

    2019  Volume 1865, Issue 1, Page(s) 158448

    Abstract: Both the endoplasmic reticulum (ER) and lipid droplets (LDs) are key players in lipid handling. In addition to this functional connection, the two organelles are also tightly linked due to the fact that the ER is the birthplace of LDs. LDs have an ... ...

    Abstract Both the endoplasmic reticulum (ER) and lipid droplets (LDs) are key players in lipid handling. In addition to this functional connection, the two organelles are also tightly linked due to the fact that the ER is the birthplace of LDs. LDs have an atypical architecture, consisting of a neutral lipid core that is covered by a phospholipid monolayer. LD biogenesis starts with neutral lipid synthesis in the ER membrane and formation of small neutral lipid lenses between its leaflets, followed by budding of mature LDs toward the cytosol. Several ER proteins have been identified that are required for efficient LD formation, among them seipin, Pex30, and FIT2. Recent evidence indicates that these LD biogenesis factors might cooperate with specific lipids, thus generating ER subdomains optimized for LD assembly. Intriguingly, LD biogenesis reacts dynamically to nutrient stress, resulting in a spatial reorganization of LD formation in the ER.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Lipid Droplets/metabolism ; Membrane Proteins/metabolism ; Vacuoles/metabolism
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2019-04-24
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 60-7
    ISSN 1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbalip.2019.04.008
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