UBXN7

Last update 08 May 2025

Basic Info

Synonyms

KIAA0794, UBX domain protein 7, UBX domain-containing protein 7

+ [2]

Introduction

Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.

100 Clinical Results associated with UBXN7

100 Translational Medicine associated with UBXN7

0 Patents (Medical) associated with UBXN7

Literatures (Medical) associated with UBXN7

01 Jul 2024·3 Biotech

Functional transcriptome analysis revealed major changes in pathways affecting systems biology of Tharparkar cattle under seasonal heat stress

Article

Author: Gowane, Gopal R ; Dutta, Gaurav ; Singh, Ayushi ; Ludri, Ashutosh ; Verma, Archana ; Alex, Rani

Heat stress significantly disturbs the production, reproduction, and systems biology of dairy cattle. A complex interaction among biological systems helps to combat and overcome heat stress. Indicine cattle breed Tharparkar has been well known for its thermal adaptability. Therefore, present investigation considered RNA-seq technology to explore the functional transcriptomics of Tharparkar cattle with the help of samples collected in spring and summer season. Among differentially expressed genes, about 3280 genes were highly dysregulated, in which 1207 gene were upregulated and 2073 genes were downregulated (|log2fold change|≥ 1 and p ≤ 0.05). Upregulated genes were related to insulin activation, interferons, and potassium ion transport. In contrast, downregulated genes were related to RNA processing, translation, and ubiquitination. Functional annotation revealed that the pathways associated with nervous system (NPFFR1, ROBO3) and metal ion transport (KCNG2, ATP1A2) were highly activated while mRNA processing and translation (EIF4A, EIF4B) and protein processing pathway (VPS4B, PEX13) were highly downregulated. Protein-protein interactions identified hub genes such as ATP13A3, IFNGR2, UBXN7, EIF4A2, SLC12A8 found to play an important role in immune, ubiquitination, translation and transport function. Co-expression network includes LYZ, PNRC1, SQSTM1, EIF4AB and DDX17 genes which are involved in lysosomal activity, tumor inhibition, ubiquitination, and translation initiation. Chemokine signaling pathway associated with immune response was highly upregulated in cluster analysis. The findings of this study provide insights into transcriptome expression and regulation which may better explain complex thermal resilience mechanism of Tharparkar cattle in heat stress under natural conditions.Supplementary InformationThe online version contains supplementary material available at 10.1007/s13205-024-04018-2.

01 Jul 2024·iScience

Characterizing replisome disassembly in human cells

Article

Author: Ruiz, Joaquin Herrero ; Romero, Francisco ; Scaramuzza, Shaun ; Henklewska, Marta ; Nath, Sarmi ; Gambus, Agnieszka ; Liu, Chaoyu ; Jones, Rebecca M ; Bristow, Robert G ; Kanemaki, Masato T ; Natsume, Toyoaki

To ensure timely duplication of the entire eukaryotic genome, thousands of replication machineries (replisomes) act on genomic DNA at any time during S phase. In the final stages of this process, replisomes are unloaded from chromatin. Unloading is driven by polyubiquitylation of MCM7, a subunit of the terminated replicative helicase, and processed by p97/VCP segregase. Most of our knowledge of replication termination comes from model organisms, and little is known about how this process is executed and regulated in human somatic cells. Here we show that replisome disassembly in this system requires CUL2^LRR1-driven MCM7 ubiquitylation, p97, and UBXN7 for unloading and provide evidence for "backup" mitotic replisome disassembly, demonstrating conservation of such mechanisms. Finally, we find that small-molecule inhibitors against Cullin ubiquitin ligases (CULi) and p97 (p97i) affect replisome unloading but also lead to induction of replication stress in cells, which limits their usefulness to specifically target replisome disassembly processes.

07 Apr 2023·BMC biology

The UAS thioredoxin-like domain of UBXN7 regulates E3 ubiquitin ligase activity of RNF111/Arkadia.

Article

Author: Levy, Laurence ; Prunier, Celine ; Chouchene, Mouna ; Dingli, Florent ; Colasse, Sabrina ; Loew, Damarys ; Boeda, Batiste ; Amhaz, Sadek ; Henri, Julien

BACKGROUNDE3 ubiquitin ligases play critical roles in regulating cellular signaling pathways by inducing ubiquitylation of key components. RNF111/Arkadia is a RING E3 ubiquitin ligase that activates TGF-β signaling by inducing ubiquitylation and proteasomal degradation of the transcriptional repressor SKIL/SnoN. In this study, we have sought to identify novel regulators of the E3 ubiquitin ligase activity of RNF111 by searching for proteins that specifically interacts with its RING domain.RESULTSWe found that UBXN7, a member of the UBA-UBX family, directly interacts with the RING domain of RNF111 or its related E3 RNF165/ARK2C that shares high sequence homology with RNF111. We showed that UBXN7 docks on RNF111 or RNF165 RING domain through its UAS thioredoxin-like domain. Overexpression of UBXN7 or its UAS domain increases endogenous RNF111, while an UBXN7 mutant devoid of UAS domain has no effect. Conversely, depletion of UBXN7 decreases RNF111 protein level. As a consequence, we found that UBXN7 can modulate degradation of the RNF111 substrate SKIL in response to TGF-β signaling. We further unveiled this mechanism of regulation by showing that docking of the UAS domain of UBXN7 inhibits RNF111 ubiquitylation by preventing interaction of the RING domain with the E2 conjugating enzymes. By analyzing the interactome of the UAS domain of UBXN7, we identified that it also interacts with the RING domain of the E3 TOPORS and similarly regulates its E3 ubiquitin ligase activity by impairing E2 binding.CONCLUSIONSTaken together, our results demonstrate that UBXN7 acts as a direct regulator for the E3 ubiquitin ligases RNF111, RNF165, and TOPORS and reveal that a thioredoxin-like domain can dock on specific RING domains to regulate their E3 ubiquitin ligase activity.

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UBXN7

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