Ask about this productRelated genes to: UBR7 antibody
- Gene:
- UBR7 NIH gene
- Name:
- ubiquitin protein ligase E3 component n-recognin 7 (putative)
- Previous symbol:
- C14orf130
- Synonyms:
- -
- Chromosome:
- 14q32.12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-28
- Date modifiied:
- 2014-11-19
Related products to: UBR7 antibody
Related articles to: UBR7 antibody
- Insect-borne plant viruses pose a serious threat to global crop production. Melon thrips, Thrips palmi Karny, transmits tospoviruses such as groundnut bud necrosis virus (GBNV) in a persistent propagative manner. Identifying thrips genes that regulate tospovirus transmission is crucial for developing targeted management strategies; however, these genes remain poorly characterized. The present study investigated the functional role of a candidate gene of T. palmi, E3 ubiquitin-protein ligase component N-recognin 7 (E3-UBR7), in the transmission of GBNV. Expression of the E3-UBR7 transcript was altered in a life-stage-specific manner, with the highest activity 11.31-fold in adults, and less during larval stages. Oral delivery of double-stranded RNA targeting E3-UBR7 (dsE3-UBR7, 10 μg/mL, 48 h) resulted in up to 6.15-fold suppression of target gene expression in adults. Silencing induced moderate adult mortality, with no notable mortality in larvae. Exposure of dsE3-UBR7 prior to virus acquisition in the larval stage did not show a significant effect on the virus copies in T. palmi larvae (1.59 × 10 copies) and adults (1.15 × 10 copies). There was also no significant alteration in the expression of the target gene in pre-acquisition dsRNA exposure. Conversely, post- virus acquisition silencing of E3-UBR7 during the adult stage markedly reduced GBNV titre (1.53 × 10 copies), indicating suppression of viral replication. GBNV copies decreased up to 104 times in adults exposed to dsE3-UBR7. Post-acquisition silencing of E3-UBR7 was more effective in suppressing virus transmission to healthy plants (15.66 %) by T. palmi adults. The results identified E3-UBR7 as a key regulatory gene influencing GBNV transmission by T. palmi, offering a promising molecular target for management of thrips-transmitted tospoviruses. - Source: PubMed
Publication date: 2026/01/11
Rakesh VGhosh Amalendu - The N-degron pathway contributes to proteolysis by targeting N-terminal residues of destabilized proteins via E3 ligases that contain a UBR-box domain. Emerging evidence suggests the UBR-box family of E3 ubiquitin ligases (UBR1-7) is involved in the positive regulation of skeletal muscle mass. The purpose of this study was to explore the role of UBR-box E3 ubiquitin ligases under enhanced protein synthesis and skeletal muscle growth conditions. Cohorts of adult male mice were electroporated with constitutively active Akt (Akt-CA) or UBR5 RNAi constructs with a rapamycin diet intervention for 7 and 30 days, respectively. In addition, the UBR-box family was studied during the regrowth phase after nerve crush-induced inactivity. Skeletal muscle growth with Akt-CA or regrowth following inactivity increased protein abundance of UBR1, UBR2, UBR4, UBR5, and UBR7. This occurred with corresponding increases in Akt-mTORC1/S6K and MAPK/p90RSK signaling and protein synthesis. The increases in UBR-box E3s, ubiquitination, and proteasomal activity occurred independently of mTORC1 activity and were associated with increases in markers related to autophagy, ER-stress, and protein quality control pathways. Finally, while UBR5 knockdown (KD) evokes atrophy, it occurs together with hyperactivation of mTORC1 and protein synthesis. In UBR5 KD muscles, we identified an increase in protein abundance for UBR2, UBR4, and UBR7, which may highlight a compensatory response to maintain proteome integrity. Future studies will seek to understand the role of UBR-box E3s toward protein quality control in skeletal muscle plasticity. Novel UBR-box E3 ubiquitin ligases are responsive to heightened protein synthesis and alterations in skeletal muscle mass and fiber size, to maintain proteome integrity. - Source: PubMed
Publication date: 2025/10/13
Baehr Leslie MOliveira de Sousa Luis GustavoGoodman Craig ASharples Adam PWaddell David SBodine Sue CHughes David C - Macroautophagy/autophagy is a highly conserved catabolic pathway in eukaryotes that mediates the selective degradation and recycling of cellular components through the formation of double-membrane autophagosomes. ATG8 is a core component of autophagy and determines cargo selectivity through interactions with specific cargo receptors. Higher plants harbor multiple ATG8 isoforms, implying potential functional diversification; however, the biological significance of this isoform expansion remains largely unexplored. In a recent study, we identified UBR7 (UBIQUITIN PROTEIN LIGASE E3 COMPONENT N-RECOGNIN 7) as a novel N-recognin that targets ATG8a for proteasomal degradation via the Arg/N-degron pathway. This selective degradation triggers isoform switching by enabling the replacement of ATG8a with alternative ATG8 isoforms. Notably, this process occurs specifically during the recovery phase following heat stress and plays a critical role in enhancing thermotolerance. Our findings provide new insights into the functional specialization and dynamic regulation of ATG8 isoforms in plants and suggest new directions for improving crop resilience under climate-associated temperature fluctuations. HS, heat stress: HSP, heat shock protein; RBP, RNA-binding protein; UTR, untranslated region. - Source: PubMed
Publication date: 2025/08/30
Kim Seu HaPark Ohkmae K - The N-degron pathway contributes to proteolysis by targeting N-terminal residues of destabilized proteins via E3 ligases that contain a UBR-box domain. Emerging evidence suggests the UBR-box family of E3 ubiquitin ligases (UBR1-7) are involved in the positive regulation of skeletal muscle mass. The purpose of this study was to explore the role of UBR-box E3 ubiquitin ligases under enhanced protein synthesis and skeletal muscle growth conditions. Cohorts of adult male mice were electroporated with constitutively active Akt (Akt-CA) or UBR5 RNAi constructs with a rapamycin diet intervention for 7 and 30 days, respectively. In addition, the UBR-box family was studied during the regrowth phase post nerve crush induced inactivity. Skeletal muscle growth with Akt-CA or regrowth following inactivity increased protein abundance of UBR1, UBR2, UBR4, UBR5 and UBR7. This occurred with corresponding increases in Akt-mTORC1/S6K and MAPK/p90RSK signaling and protein synthesis. The increases in UBR-box E3s, ubiquitination, and proteasomal activity occurred independently of mTORC1 activity and were associated with increases in markers related to autophagy, ER-stress, and protein quality control pathways. Finally, while UBR5 knockdown (KD) evokes atrophy, it occurs together with hyperactivation of mTORC1 and protein synthesis. In UBR5 KD muscles, we identified an increase in protein abundance for UBR2, UBR4 and UBR7, which may highlight a compensatory response to maintain proteome integrity. Future studies will seek to understand the role of UBR-box E3s towards protein quality control in skeletal muscle plasticity. - Source: PubMed
Publication date: 2025/10/02
Baehr Leslie Mde Sousa Luis Gustavo OliveiraGoodman Craig ASharples Adam PWaddell David SBodine Sue CHughes David C - Autophagy is a vital process that enables plants to adapt to various environmental changes. During heat stress (HS), misfolded and denatured proteins accumulate in cells, necessitating autophagy for their removal. Here, we show that a core autophagy component ATG8a is targeted for degradation via the Arg/N-degron pathway. ATG8a is expressed as two alternatively spliced transcripts encoding ATG8a isoforms, namely ATG8a(S) and ATG8a(L), with distinct N-termini. While ATG8a(S) remains stable, ATG8a(L) is N-terminally processed to expose the Arg/N-degron, leading to its degradation. Ubiquitin protein ligase E3 component N-recognin 7 (UBR7), identified as an N-recognin, is responsible for ubiquitination and proteasomal degradation of ATG8a(L). Notably, ATG8a(S) and ATG8a(L) show dynamic expression patterns, fluctuating ATG8a levels during the HS and recovery periods. Our findings highlight the crucial role of ATG8a turnover in conferring thermotolerance, which is governed by Arg/N-degron-mediated regulation. Understanding the molecular basis of ATG8a stability will provide valuable insights into plant resilience to HS under changing climatic conditions. - Source: PubMed
Publication date: 2025/07/01
Kim Seu HaPark Jun SeokLee Myoung-HoonSeo JoongyuKim JaekwanYang Woo SeokPark JihyeYoo KwangminChoi JungminSeo Jong-BokSong Hyun KyuPark Ohkmae K