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  1. Article ; Online: Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space.

    Lolicato, Fabio / Steringer, Julia P / Saleppico, Roberto / Beyer, Daniel / Fernandez-Sobaberas, Jaime / Unger, Sebastian / Klein, Steffen / Riegerová, Petra / Wegehingel, Sabine / Müller, Hans-Michael / Schmitt, Xiao J / Kaptan, Shreyas / Freund, Christian / Hof, Martin / Šachl, Radek / Chlanda, Petr / Vattulainen, Ilpo / Nickel, Walter

    eLife

    2024  Volume 12

    Abstract: Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5) ... ...

    Abstract Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5)P
    MeSH term(s) Extracellular Space ; Dimerization ; Fibroblast Growth Factor 2 ; Sodium-Potassium-Exchanging ATPase ; Disulfides
    Chemical Substances Fibroblast Growth Factor 2 (103107-01-3) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; Disulfides
    Language English
    Publishing date 2024-01-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.88579
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Physiological and metabolomic consequences of reduced expression of the Drosophila brummer triglyceride Lipase.

    Nazario-Yepiz, Nestor O / Fernández Sobaberas, Jaime / Lyman, Roberta / Campbell, Marion R / Shankar, Vijay / Anholt, Robert R H / Mackay, Trudy F C

    PloS one

    2021  Volume 16, Issue 9, Page(s) e0255198

    Abstract: Disruption of lipolysis has widespread effects on intermediary metabolism and organismal phenotypes. Defects in lipolysis can be modeled in Drosophila melanogaster through genetic manipulations of brummer (bmm), which encodes a triglyceride lipase ... ...

    Abstract Disruption of lipolysis has widespread effects on intermediary metabolism and organismal phenotypes. Defects in lipolysis can be modeled in Drosophila melanogaster through genetic manipulations of brummer (bmm), which encodes a triglyceride lipase orthologous to mammalian Adipose Triglyceride Lipase. RNAi-mediated knock-down of bmm in all tissues or metabolic specific tissues results in reduced locomotor activity, altered sleep patterns and reduced lifespan. Metabolomic analysis on flies in which bmm is downregulated reveals a marked reduction in medium chain fatty acids, long chain saturated fatty acids and long chain monounsaturated and polyunsaturated fatty acids, and an increase in diacylglycerol levels. Elevated carbohydrate metabolites and tricarboxylic acid intermediates indicate that impairment of fatty acid mobilization as an energy source may result in upregulation of compensatory carbohydrate catabolism. bmm downregulation also results in elevated levels of serotonin and dopamine neurotransmitters, possibly accounting for the impairment of locomotor activity and sleep patterns. Physiological phenotypes and metabolomic changes upon reduction of bmm expression show extensive sexual dimorphism. Altered metabolic states in the Drosophila model are relevant for understanding human metabolic disorders, since pathways of intermediary metabolism are conserved across phyla.
    MeSH term(s) Animals ; Drosophila Proteins/antagonists & inhibitors ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/physiology ; Female ; Lipase/antagonists & inhibitors ; Lipase/genetics ; Lipase/metabolism ; Locomotion ; Longevity ; Male ; Metabolome ; Neurotransmitter Agents/metabolism ; RNA Interference ; Sex Characteristics ; Sleep/physiology
    Chemical Substances Drosophila Proteins ; Neurotransmitter Agents ; Lipase (EC 3.1.1.3) ; BMM protein, Drosophila (EC 3.1.1.3.)
    Language English
    Publishing date 2021-09-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0255198
    Database MEDical Literature Analysis and Retrieval System OnLINE

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