publication . Article . Other literature type . 2010

Ancient Ubiquitous Protein 1 (AUP1) Localizes to Lipid Droplets and Binds the E2 Ubiquitin Conjugase G2 (Ube2g2) via Its G2 Binding Region

Spandl, Johanna; Lohmann, Daniel; Kuerschner, Lars; Moessinger, Christine; Thiele, Christoph;
Open Access
  • Published: 02 Dec 2010 Journal: Journal of Biological Chemistry, volume 286, pages 5,599-5,606 (issn: 0021-9258, eissn: 1083-351X, Copyright policy)
  • Publisher: American Society for Biochemistry & Molecular Biology (ASBMB)
Abstract
Lipid droplets (LDs), the major intracellular storage sites for neutral lipids, consist of a neutral lipid core surrounded by a phospholipid monolayer membrane. In addition to their function in lipid storage, LDs participate in lipid biosynthesis and recently were implicated in proteasomal protein degradation and autophagy. To identify components of the protein degradation machinery on LDs, we studied several candidates identified in previous LD proteome analyses. Here, we demonstrate that the highly conserved and broadly expressed ancient ubiquitous protein 1 (AUP1) localizes to LDs, where it integrates into the LD surface in a monotopic fashion with both termi...
Subjects
free text keywords: Cell Biology, Biochemistry, Molecular Biology, AUP1, Protein degradation, Ubiquitin-conjugating enzyme, Lipid droplet, Ubiquitin, biology.protein, biology, Cytosol, Lipid biosynthesis, Plasma protein binding
Funded by
EC| LIPIDOMICNET
Project
LIPIDOMICNET
Lipid droplets as dynamic organelles of fat deposition and release: Translational research towards human disease
  • Funder: European Commission (EC)
  • Project Code: 202272
  • Funding stream: FP7 | SP1 | HEALTH
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