ArticleThe Biochemical journal2006
Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.
- Meta-analysis of Ubiquilin1 gene polymorphism and Alzheimer's disease risk.Medical science monitor : international medical journal of experimental and clinical research · 2014Pooled it
- UBQLN2 is necessary for UBE3A-mediated proteasomal degradation of the domesticated retroelement PEG10.Journal of cell science · 2025Article
- Ion Mobility Mass Spectrometry Unveils Global Protein Conformations in Response to Conditions that Promote and Reverse Liquid-Liquid Phase Separation.Journal of the American Chemical Society · 2023Article
- UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding.Biochimica et biophysica acta. General subjects · 2023Article
- Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly.Science (New York, N.Y.) · 2021Article
- Ubiquitin-Modulated Phase Separation of Shuttle Proteins: Does Condensate Formation Promote Protein Degradation?BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Review
- Structure, dynamics and functions of UBQLNs: at the crossroads of protein quality control machinery.The Biochemical journal · 2020Review
- ALS/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions.Molecular cell · 2018Article
- Mutation-dependent aggregation and toxicity in a Drosophila model for UBQLN2-associated ALS.Human molecular genetics · 2018Article
- Article
- The STI and UBA Domains of UBQLN1 Are Critical Determinants of Substrate Interaction and Proteostasis.Journal of cellular biochemistry · 2017Article
- Investigation of the adaptor protein PLIC-2 in multiple pathways.Biochemistry and biophysics reports · 2017Article
- Pathogenic Ubqln2 gains toxic properties to induce neuron death.Acta neuropathologica · 2015Article
- Signature changes in ubiquilin expression in the R6/2 mouse model of Huntington's disease.Brain research · 2015Article
- Ubiquilin 2 is not associated with tau pathology.PloS one · 2013Article
- UBQLN1 interacts with SPEM1 and participates in spermiogenesis.Molecular and cellular endocrinology · 2010Article
- TDP-43 dimerizes in human cells in culture.Cellular and molecular neurobiology · 2010Article
- Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation.Cellular and molecular life sciences : CMLS · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquilin proteins have been shown to interact with a wide variety of other cellular proteins, often regulating the stability and degradation of the interacting protein. Ubiquilin contains a UBL (ubiquitin-like) domain at the N-terminus and a UBA (ubiquitin-associated) domain at the C-terminus, separated by a central region containing Sti1-like repeats. Little is known about regulation of the interaction of ubiquilin with other proteins. In the present study, we show that ubiquilin is capable of forming dimers, and that dimerization requires the central region of ubiquilin, but not its UBL or the UBA domains. Furthermore, we provide evidence suggesting that monomeric ubiquilin is likely to be the active form that is involved in binding presenilin proteins. Our results provide new insight into the regulatory mechanism underlying the interaction of ubiquilin with presenilins.
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What OpenQuestion holds
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.