Dual Role of Ancient Ubiquitous Protein 1 (AUP1) in Lipid Droplet Accumulation and Endoplasmic Reticulum (ER) Protein Quality Control
Published 2011 View Full Article
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Title
Dual Role of Ancient Ubiquitous Protein 1 (AUP1) in Lipid Droplet Accumulation and Endoplasmic Reticulum (ER) Protein Quality Control
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 43, Pages 37602-37614
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2011-08-23
DOI
10.1074/jbc.m111.284794
References
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Note: Only part of the references are listed.- Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1p
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- Huntingtin Interacts with the Cue Domain of gp78 and Inhibits gp78 Binding to Ubiquitin and p97/VCP
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- (2009) Z. Kostova et al. JOURNAL OF CELL SCIENCE
- Allosteric Activation of E2-RING Finger-Mediated Ubiquitylation by a Structurally Defined Specific E2-Binding Region of gp78
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- Ancient ubiquitous protein 1 and Syk link cytoplasmic tails of the integrinαIIbβ3
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- A Dual Task for the Xbp1-responsive OS-9 Variants in the Mammalian Endoplasmic Reticulum
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- Cue1p Is an Activator of Ubc7p E2 Activityin Vitroandin Vivo
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- Gp78 Cooperates with RMA1 in Endoplasmic Reticulum-associated Degradation of CFTRΔF508
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- Functional genomic screen reveals genes involved in lipid-droplet formation and utilization
- (2008) Yi Guo et al. NATURE
- OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
- (2008) John C. Christianson et al. NATURE CELL BIOLOGY
- SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
- (2008) B. Mueller et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole
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