| FAT10 and NUB1L cooperate to activate the 26S proteasome. | FAT10 and NUB1L cooperate to activate the 26S proteasome.
Brockmann F, Catone N, Wünsch C, Offensperger F, Scheffner M, Schmidtke G, Aichem A., Free PMC Article | 05/25/2023 |
| SNHG12 regulates biological behaviors of ox-LDL-induced HA-VSMCs through upregulation of SPRY2 and NUB1. | SNHG12 regulates biological behaviors of ox-LDL-induced HA-VSMCs through upregulation of SPRY2 and NUB1.
Jiang W, Zhao W, Ye F, Huang S, Wu Y, Chen H, Zhou R, Fu G. | 02/5/2022 |
| Overexpression of negative regulator of ubiquitin-like proteins 1 (NUB1) inhibits proliferation and invasion of gastric cancer cells through upregulation of p27Kip1 and inhibition of epithelial-mesenchymal transition. | Overexpression of negative regulator of ubiquitin-like proteins 1 (NUB1) inhibits proliferation and invasion of gastric cancer cells through upregulation of p27Kip1 and inhibition of epithelial-mesenchymal transition.
Zhang D, Wu P, Zhang Z, An W, Zhang C, Pan S, Tan Y, Xu H. | 05/15/2021 |
| Authors created a series of phosphomimic mutants of NUB1 and found that phosphorylation of NUB1 at S46 (P-NUB46) efficiently degrades aggregates using a cell-based assay. | Phosphorylated NUB1 distinguishes α-synuclein in Lewy bodies from that in glial cytoplasmic inclusions in multiple system atrophy.
Tanji K, Miki Y, Mori F, Kon T, Kakita A, Takahashi H, Wakabayashi K., Free PMC Article | 04/11/2020 |
| Mdm2 acts as a positive regulator of NUB1 function, by modulating NUB1 ubiquitination on lysine 159. | Regulation of NUB1 Activity through Non-Proteolytic Mdm2-Mediated Ubiquitination.
Bonacci T, Audebert S, Camoin L, Baudelet E, Iovanna JL, Soubeyran P., Free PMC Article | 08/12/2017 |
| data suggest that NUB1 participates in telomere maintenance by regulating the levels of TRF1 at telomeres through both NEDD8-dependent and NEDD8-independent pathways. | NEDD8 ultimate buster-1 regulates the abundance of TRF1 at telomeres by promoting its proteasomal degradation.
Jeong YY, Her J, Chung IK. | 04/29/2017 |
| NUB1L suppresses atypical neddylation and promotes the degradation of misfolded proteins by the proteasome | NEDD8 Ultimate Buster 1 Long (NUB1L) Protein Suppresses Atypical Neddylation and Promotes the Proteasomal Degradation of Misfolded Proteins.
Li J, Ma W, Li H, Hou N, Wang X, Kim IM, Li F, Su H., Free PMC Article | 12/19/2015 |
| Based on biochemical features of the VBM motifs, we also identified NUB1L (NEDD8 ultimate buster-1 long) as a novel VBM-containing protein, which is involved in proteasomal degradation of NEDD8 through the P97 pathway. | Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97/VCP.
Liu S, Fu QS, Zhao J, Hu HY. | 02/22/2014 |
| In coordination with the P97-UFD1-NPL4 complex (P97(UFD1/NPL4)), NUB1L promotes transfer of NEDD8 to proteasome for degradation. | NEDD8 ultimate buster-1 long (NUB1L) protein promotes transfer of NEDD8 to proteasome for degradation through the P97UFD1/NPL4 complex.
Liu S, Yang H, Zhao J, Zhang YH, Song AX, Hu HY., Free PMC Article | 01/4/2014 |
| This study identified genes modifying endogenous mHTT using high-throughput screening and demonstrate NUB1 as an exemplar entry point for therapeutic intervention of Huntington's disease. | Identification of NUB1 as a suppressor of mutant Huntington toxicity via enhanced protein clearance.
Lu B, Al-Ramahi I, Valencia A, Wang Q, Berenshteyn F, Yang H, Gallego-Flores T, Ichcho S, Lacoste A, Hild M, Difiglia M, Botas J, Palacino J. | 06/29/2013 |
| Data propose that NUB1, by regulating GSK3beta levels, modulates tau phosphorylation and aggregation, and is a key player in neurodegeneration associated with tau pathology. | NUB1 modulation of GSK3β reduces tau aggregation.
Richet E, Pooler AM, Rodriguez T, Novoselov SS, Schmidtke G, Groettrup M, Hanger DP, Cheetham ME, van der Spuy J. | 06/1/2013 |
| In the present study, the proportions of intranuclear inclusion positive for NEDD8, NUB1 and SUMO-1 were significantly lower in glial cells than in neurons. | Ubiquitin-related proteins in neuronal and glial intranuclear inclusions in intranuclear inclusion body disease.
Mori F, Tanji K, Odagiri S, Hattori M, Hoshikawa Y, Kono C, Yasui K, Yokoi S, Hasegawa Y, Kamitani T, Yoshida M, Wakabayashi K. | 09/22/2012 |
| findings show how FAT10 and NUB1L dock with the 26S proteasome to initiate proteolysis; identified the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2. | FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis.
Rani N, Aichem A, Schmidtke G, Kreft SG, Groettrup M. | 08/4/2012 |
| The finding of this study suggested that NUB1 along with abnormal alpha-synuclein is involved in the pathogenesis of Lewy body disease. | Synphilin-1-binding protein NUB1 is colocalized with nonfibrillar, proteinase K-resistant α-synuclein in presynapses in Lewy body disease.
Tanji K, Mori F, Kito K, Kakita A, Mimura J, Itoh K, Takahashi H, Kamitani T, Wakabayashi K., Free PMC Article | 11/19/2011 |
| NUB1L not only acts as a linker between the 26 S proteasome and ubiquitin-like proteins, but also as a facilitator of proteasomal degradation. | The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10.
Schmidtke G, Kalveram B, Weber E, Bochtler P, Lukasiak S, Hipp MS, Groettrup M. | 01/21/2010 |
| The inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1 in the retina. | The inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1.
Akey DT, Zhu X, Dyer M, Li A, Sorensen A, Blackshaw S, Fukuda-Kamitani T, Daiger SP, Craft CM, Kamitani T, Sohocki MM., Free PMC Article | 01/21/2010 |
| interaction between NUB1 and AIPL1 is affected in patients with Leber congenital amaurosis | Abolished interaction of NUB1 with mutant AIPL1 involved in Leber congenital amaurosis.
Kanaya K, Sohocki MM, Kamitani T. | 01/21/2010 |
| These results suggest that NUB1 indeed targets synphilin-1 to the proteasome for its efficient degradation, which, because of the resultant reduction in synphilin-1, suppresses the formation of synphilin-1-positive inclusions. | NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1.
Tanji K, Tanaka T, Mori F, Kito K, Takahashi H, Wakabayashi K, Kamitani T., Free PMC Article | 01/21/2010 |
| These results imply that the ubiquitin precursor UbC1 hydrolysis mediated by NEDD8 ultimate buster-1 (NUB1) is involved in cellular functions in the seminiferous tubules such as spermatogenesis. | NUB1-mediated targeting of the ubiquitin precursor UbC1 for its C-terminal hydrolysis.
Tanaka T, Yeh ET, Kamitani T. | 01/21/2010 |
| Data show that aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) can modulate protein translocation and act in a chaperone-like manner and suggest that AIPL1 is an important modulator of NEDD8 ultimate buster protein 1 (NUB1) cellular function. | The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments.
van der Spuy J, Cheetham ME. | 01/21/2010 |
| NUB1 has a splicing variant, NUB1L, which regulates the NEDD8 conjugation system | Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L.
Tanaka T, Kawashima H, Yeh ET, Kamitani T. | 01/21/2010 |