Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 535505
Title Hypoxia-inducible lipid droplet-associated protein inhibits adipose triglyceride lipase
Author(s) Padmanabha Das, Krishna M.; Wechselberger, Lisa; Liziczai, Márton; La Rosa Rodriguez, Montserrat De; Grabner, Gernot F.; Heier, Christoph; Viertlmayr, Roland; Radler, Claudia; Lichtenegger, Jörg; Zimmermann, Robert; Borst, Jan Willem; Zechner, Rudolf; Kersten, Sander; Oberer, Monika
Source Journal of Lipid Research 59 (2018)3. - ISSN 0022-2275 - p. 531 - 541.
Department(s) Chair Nutrition Metabolism and Genomics
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) Adipocytes - Hypoxia-inducible gene-2 - Intracellular lipolysis - Lipolysis and fatty acid metabolism - Triglycerides
Abstract Elaborate control mechanisms of intracellular triacylglycerol (TAG) breakdown are critically involved in the maintenance of energy homeostasis. Hypoxia-inducible lipid droplet-associated protein (HILPDA)/hypoxia-inducible gene-2 (Hig-2) has been shown to affect intracellular TAG levels, yet, the underlying molecular mechanisms are unclear. Here, we show that HILPDA inhibits adipose triglyceride lipase (ATGL), the enzyme catalyzing the first step of intracellular TAG hydrolysis. HILPDA shares structural similarity with G0/G1 switch gene 2 (G0S2), an established inhibitor of ATGL. HILPDA inhibits ATGL activity in a dose-dependent manner with an IC50 value of ∼2 μM. ATGL inhibition depends on the direct physical interaction of both proteins and involves the N-terminal hydrophobic region of HILPDA and the N-terminal patatin domain-containing segment of ATGL. Finally, confocal microscopy combined with Förster resonance energy transfer-fluorescence lifetime imaging microscopy analysis indicated that HILPDA and ATGL colocalize and physically interact intracellularly. These findings provide a rational biochemical explanation for the tissue-specific increased TAG accumulation in HILPDA-overexpressing transgenic mouse models.
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