ArticleThe Journal of biological chemistry2012
The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate compartment.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- Unconventional Protein Transport Across the Golgi Ribbon.Sub-cellular biochemistry · 2026Review
- TUG protein acts through a disordered region to organize the early secretory pathway.Nature communications · 2025Article
- Mechanism of allosteric inhibition of human p97/VCP ATPase and its disease mutant by triazole inhibitors.Communications chemistry · 2024Article
- Exploring the role of ubiquitin regulatory X domain family proteins in cancers: bioinformatics insights, mechanisms, and implications for therapy.Journal of translational medicine · 2024Review
- ASPSCR1-TFE3 reprograms transcription by organizing enhancer loops around hexameric VCP/p97.Nature communications · 2024Article
- The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions.Nature structural & molecular biology · 2023Article
- The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL.FEBS open bio · 2023Article
- Structural basis for recognition and methylation of p97 by METTL21D, a valosin-containing protein lysine methyltransferase.iScience · 2023Article
- Structural remodeling of AAA+ ATPase p97 by adaptor protein ASPL facilitates posttranslational methylation by METTL21D.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- GA signaling expands: The plant UBX domain-containing protein 1 is a binding partner for the GA receptor.Plant physiology · 2022Article
- Cryo-EM structures of human p97 double hexamer capture potentiated ATPase-competent state.Cell discovery · 2022Article
- The p97 Inhibitor UPCDC-30245 Blocks Endo-Lysosomal Degradation.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Ubiquitin-like processing of TUG proteins as a mechanism to regulate glucose uptake and energy metabolism in fat and muscle.Frontiers in endocrinology · 2022Review
- Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation.iScience · 2021Article
- Insulin-stimulated endoproteolytic TUG cleavage links energy expenditure with glucose uptake.Nature metabolism · 2021Article
- Domain Organization of the UBX Domain Containing Protein 9 and Analysis of Its Interactions With the Homohexameric AAA + ATPase p97 (Valosin-Containing Protein).Frontiers in cell and developmental biology · 2021Article
- CHC22 clathrin mediates traffic from early secretory compartments for human GLUT4 pathway biogenesis.The Journal of cell biology · 2020Article
- GLUT4 Storage Vesicles: Specialized Organelles for Regulated Trafficking.The Yale journal of biology and medicine · 2019Review
- Acylation - A New Means to Control Traffic Through the Golgi.Frontiers in cell and developmental biology · 2019Review
- The AAA+ ATPase p97, a cellular multitool.The Biochemical journal · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
p97/VCP is a hexameric ATPase that is coupled to diverse cellular processes, such as membrane fusion and proteolysis. How p97 activity is regulated is not fully understood. Here we studied the potential role of TUG, a widely expressed protein containing a UBX domain, to control mammalian p97. In HEK293 cells, the vast majority of TUG was bound to p97. Surprisingly, the TUG UBX domain was neither necessary nor sufficient for this interaction. Rather, an extended sequence, comprising three regions of TUG, bound to the p97 N-terminal domain. The TUG C terminus resembled the Arabidopsis protein PUX1. Similar to the previously described action of PUX1 on AtCDC48, TUG caused the conversion of p97 hexamers into monomers. Hexamer disassembly was stoichiometric rather than catalytic and was not greatly affected by the p97 ATP-binding state or by TUG N-terminal regions in vitro. In HeLa cells, TUG localized to the endoplasmic reticulum-to-Golgi intermediate compartment and endoplasmic reticulum exit sites. Although siRNA-mediated TUG depletion had no marked effect on total ubiquitylated proteins or p97 localization, TUG overexpression caused an accumulation of ubiquitylated substrates and targeted both TUG and p97 to the nucleus. A physiologic role of TUG was revealed by siRNA-mediated depletion, which showed that TUG is required for efficient reassembly of the Golgi complex after brefeldin A removal. Together, these data support a model in which TUG controls p97 oligomeric status at a particular location in the early secretory pathway and in which this process regulates membrane trafficking in various cell types.
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