ArticleJournal of lipid research2013
Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1.
Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Navigating lipid droplet proteins - part II: molecular mechanisms underlying ER-to-lipid droplet protein partitioning.Biochemical Society transactions · 2025Review
- Cyanoglobule lipid droplets are a stress-responsive metabolic compartment of cyanobacteria and the progenitor of plant plastoglobules.The Plant cell · 2025Article
- AUP1 and UBE2G2 complex targets STING signaling and regulates virus-induced innate immunity.mBio · 2025Article
- Hairpin protein partitioning from the ER to lipid droplets involves major structural rearrangements.Nature communications · 2024Article
- Review
- AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and Polyubiquitination of NKCC2.Cells · 2024Article
- AUP1 regulates lipid metabolism and induces lipid accumulation to accelerate the progression of renal clear cell carcinoma.Cancer science · 2022Article
- Co-translational biogenesis of lipid droplet integral membrane proteins.Journal of cell science · 2022Article
- The CYTOLD and ERTOLD pathways for lipid droplet-protein targeting.Trends in biochemical sciences · 2022Review
- A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation.PLoS biology · 2021Article
- ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.Scientific reports · 2021Article
- Picornaviruses: A View from 3A.Viruses · 2021Review
- Molecular Events Occurring in Lipophagy and Its Regulation inFrontiers in microbiology · 2021Review
- Determinants of Endoplasmic Reticulum-to-Lipid Droplet Protein Targeting.Developmental cell · 2020Article
- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- Proteomic analysis of monolayer-integrated proteins on lipid droplets identifies amphipathic interfacial α-helical membrane anchors.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Infectious Bursal Disease Virus Hijacks Endosomal Membranes as the Scaffolding Structure for Viral Replication.Journal of virology · 2018Article
- Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets.Trends in cell biology · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ancient ubiquitous protein 1 (AUP1) is a multifunctional protein, which acts on both lipid droplets (LDs) and the endoplasmic reticulum (ER) membrane. Double localization to these two organelles, featuring very different membrane characteristics, was observed also for several other integral proteins, but little is known about the signals and mechanisms behind dual protein targeting to ER and LDs. Here we dissect the AUP1 targeting signals by analyses of localization and topology of several deletion and point mutants. We found that AUP1 is inserted into the membrane of the ER in a monotopic hairpin fashion, and subsequently transported to the hemi-membrane of LDs. A single domain localized in the N-terminal part of AUP1 enables its ER residence, the monotopic insertion, and the LD localization. Different specific residues within this multifunctional domain are responsible for achieving the complex spatial distribution pattern. A mutation of three amino acids, which changes AUP1 topology from hairpin to transmembrane, abolishes LD localization. These findings suggest that the cell is able to target a protein to multiple intracellular locations using a single domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.