| Structural insights into Ubr1-mediated N-degron polyubiquitination. | Structural insights into Ubr1-mediated N-degron polyubiquitination.
Pan M, Zheng Q, Wang T, Liang L, Mao J, Zuo C, Ding R, Ai H, Xie Y, Si D, Yu Y, Liu L, Zhao M., Free PMC Article | 03/5/2022 |
| Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control. | Direct involvement of Hsp70 ATP hydrolysis in Ubr1-dependent quality control.
Singh A, Vashistha N, Heck J, Tang X, Wipf P, Brodsky JL, Hampton RY., Free PMC Article | 07/17/2021 |
| Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase. | Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase.
Kong KE, Fischer B, Meurer M, Kats I, Li Z, Rühle F, Barry JD, Kirrmaier D, Chevyreva V, San Luis BJ, Costanzo M, Huber W, Andrews BJ, Boone C, Knop M, Khmelinskii A., Free PMC Article | 06/26/2021 |
| Altered substrate recognition by Ubr1 accelerates proteasomal degradation of misfolded as well as native proteins at the endoplasmic reticulum membrane and in the cytosol. We term this pathway stress-induced homeostatically regulated protein degradation (SHRED) and propose that it promotes physiological adaptation. | SHRED Is a Regulatory Cascade that Reprograms Ubr1 Substrate Specificity for Enhanced Protein Quality Control during Stress.
Szoradi T, Schaeff K, Garcia-Rivera EM, Itzhak DN, Schmidt RM, Bircham PW, Leiss K, Diaz-Miyar J, Chen VK, Muzzey D, Borner GHH, Schuck S. | 03/23/2019 |
| In addition to the E3 ubiquitin ligase Ubr1, we identified the prefoldin chaperone subunit Gim3 as an important quality control factor. We found that Gim3 interacted with the Guk1 mutant allele and propose that prefoldin promotes the degradation of the unstable model substrate by maintaining the solubility of the misfolded protein | Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.
Comyn SA, Young BP, Loewen CJ, Mayor T., Free PMC Article | 03/25/2017 |
| The major ubiquitin ligase targeting the superfluous Fas2 subunit to the proteasome is Ubr1. The ubiquitin-conjugating enzymes Ubc2 and Ubc4 assist the degradation process. | Quality control of a cytoplasmic protein complex: chaperone motors and the ubiquitin-proteasome system govern the fate of orphan fatty acid synthase subunit Fas2 of yeast.
Scazzari M, Amm I, Wolf DH., Free PMC Article | 05/9/2015 |
| Ubr1 Is Present at the endoplasmic reticulum membrane of wild-type cells and becomes a ligase for ER-associated protein degradation of Ste6* under heat and ethanol stress. | Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.
Stolz A, Besser S, Hottmann H, Wolf DH., Free PMC Article | 11/30/2013 |
| Data show that ubiquitin-protein ligases Ubr1 and Ubr2 have opposing roles in Ste11DeltaNK444R-GFP aggregation. | A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.
Theodoraki MA, Nillegoda NB, Saini J, Caplan AJ., Free PMC Article | 10/13/2012 |
| Study shows that the RING-type Ubr1 E3 and the HECT-type Ufd4 E3 interact, both physically and functionally. | The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases.
Hwang CS, Shemorry A, Auerbach D, Varshavsky A., Free PMC Article | 01/8/2011 |
| Data suggest that Ubr1 and Ubr2 represent E3 components of a novel quality control pathway for proteins synthesized on cytosolic ribosomes. | Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.
Nillegoda NB, Theodoraki MA, Mandal AK, Mayo KJ, Ren HY, Sultana R, Wu K, Johnson J, Cyr DM, Caplan AJ., Free PMC Article | 01/1/2011 |
| The UBR box, alone & in complex with N-degron peptides, has a previously unknown protein fold stabilized by a novel binuclear zinc center. N-terminal Arg, Lys or His N-degron side chains are coordinated in a multispecific binding pocket. | Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases.
Choi WS, Jeong BC, Joo YJ, Lee MR, Kim J, Eck MJ, Song HK. | 11/27/2010 |
| phenotypic and biochemical studies of Ubr1 and San1 indicate that two strategies are employed for cytoplasmic QC: chaperone-assisted ubiquitination by Ubr1 and chaperone-dependent delivery to nuclear San1 | Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1.
Heck JW, Cheung SK, Hampton RY., Free PMC Article | 03/29/2010 |
| Ubr1 is responsible for targeting misfolded cytosoplasmic protein to proteasomal degradation. | Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.
Eisele F, Wolf DH. | 01/21/2010 |
| Yck1/Yck2-mediated phosphorylation of Ubr1 on Ser(300) plays a major role in the control of peptide import by the N-end rule pathway, the subsequent (primed) phosphorylations, including the one on Tyr(277), have at most minor effects on Ubr1 | Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway.
Hwang CS, Varshavsky A., Free PMC Article | 01/21/2010 |
| analysis of functional links between the amino acids-sensing SPS system, the CUP9-TUP1-SSN6 repressor complex, the PTR2 peptide transporter, and the UBR1-dependent N-end rule pathway | Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter.
Xia Z, Turner GC, Hwang CS, Byrd C, Varshavsky A., Free PMC Article | 01/21/2010 |
| Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway | Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway.
Xia Z, Webster A, Du F, Piatkov K, Ghislain M, Varshavsky A., Free PMC Article | 01/21/2010 |