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Verfasst von:Poppelreuther, Margarete [VerfasserIn]   i
 Rudolph, Berenice Mareen [VerfasserIn]   i
 Du, Chen [VerfasserIn]   i
 Vellaramkalayil, Regina [VerfasserIn]   i
 Becker, Melanie [VerfasserIn]   i
 Ehehalt, Robert [VerfasserIn]   i
 Füllekrug, Joachim [VerfasserIn]   i
Titel:The N-terminal region of acyl-CoA synthetase 3 is essential for both the localization on lipid droplets and the function in fatty acid uptake
Verf.angabe:Margarete Poppelreuther, Berenice Rudolph, Chen Du, Regina Großmann, Melanie Becker, Christoph Thiele, Robert Ehehalt, and Joachim Füllekrug
E-Jahr:2012
Jahr:February 22, 2012
Umfang:13 S.
Fussnoten:Gesehen am 14.08.2018
Titel Quelle:Enthalten in: Journal of lipid research
Ort Quelle:Amsterdam : Elsevier, 1959
Jahr Quelle:2012
Band/Heft Quelle:53(2012), 5, Seite 888-900
ISSN Quelle:1539-7262
Abstract:Cytosolic lipid droplets (LDs) are storage organelles for neutral lipids derived from endogenous metabolism. Acyl-CoA synthetase family proteins are essential enzymes in this biosynthetic pathway, contributing activated fatty acids. Fluorescence microscopy showed that ACSL3 is localized to the endoplasmic reticulum (ER) and LDs, with the distribution dependent on the cell type and the supply of fatty acids. The N-terminus of ACSL3 was necessary and sufficient for targeting reporter proteins correctly, as demonstrated by subcellular fractionation and confocal microscopy. The N-terminal region of ACSL3 was also found to be functionally required for the enzyme activity. Selective permeabilization and in silico analysis suggest that ACSL3 assumes a hairpin membrane topology, with the N-terminal hydrophobic amino acids forming an amphipathic helix restricted to the cytosolic leaflet of the ER membrane. ACSL3 was effectively translocated from the ER to nascent LDs when neutral lipid synthesis was stimulated by the external addition of fatty acids. Cellular fatty acid uptake was increased by overexpression and reduced by RNA interference of ACSL3. In conclusion, the structural organization of ACSL3 allows the fast and efficient movement from the ER to emerging LDs. ACSL3 not only esterifies fatty acids with CoA but is also involved in the cellular uptake of fatty acids, presumably indirectly by metabolic trapping. The unique localization of the acyl-CoA synthetase ACSL3 on LDs suggests a function in the local synthesis of lipids.
DOI:doi:10.1194/jlr.M024562
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

kostenfrei: Volltext: http://dx.doi.org/10.1194/jlr.M024562
 kostenfrei: Volltext: http://www.jlr.org/content/53/5/888
 DOI: https://doi.org/10.1194/jlr.M024562
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:endoplasmic reticulum
 fluorescence microscopy
 lipid metabolism
 membrane anchor
 subcellular targeting
K10plus-PPN:157853514X
Verknüpfungen:→ Zeitschrift

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