Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Following the formation of PSMD10:PSMC4:PSMC5:PAAF1, PSMD9:P...
| Class:Id | Summation:9907989 |
|---|---|
| _displayName | Following the formation of PSMD10:PSMC4:PSMC5:PAAF1, PSMD9:P... |
| _timestamp | 2024-04-26 23:20:39 |
| created | [InstanceEdit:9907990] Orlic-Milacic, Marija, 2024-04-18 |
| literatureReference | [LiteratureReference:9907904] Molecular architecture and assembly of the eukaryotic proteasome [LiteratureReference:9908486] Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones [LiteratureReference:9908517] Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets [LiteratureReference:9908521] Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism [LiteratureReference:9908532] SUMOylation of Psmd1 controls Adrm1 interaction with the proteasome [LiteratureReference:9908526] A High Affinity hRpn2-Derived Peptide That Displaces Human Rpn13 from Proteasome in 293T Cells [LiteratureReference:5689596] A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes [LiteratureReference:9908520] Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2 [LiteratureReference:9908533] Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13 |
| modified | [InstanceEdit:9908515] Orlic-Milacic, Marija, 2024-04-22 [InstanceEdit:9908538] Orlic-Milacic, Marija, 2024-04-22 [InstanceEdit:9908560] Orlic-Milacic, Marija, 2024-04-22 [InstanceEdit:9908897] Orlic-Milacic, Marija, 2024-04-23 [InstanceEdit:9908898] Orlic-Milacic, Marija, 2024-04-23 [InstanceEdit:9909124] Orlic-Milacic, Marija, 2024-04-26 |
| text | Following the formation of PSMD10:PSMC4:PSMC5:PAAF1, PSMD9:PSMC3:PSCM6, and PSMD5:PSMC2:PSMC1:PSMD2 modules of the base of the proteasome 19S regulatory particle (19S RP), they associate with one another, along with binding of PSMD1 (ortholog of yeast Rpn2) and ADRM1 (ortholog of yeast Rpn13), and release of PSMD9 (Nas2/p27), to form the base precursor. ATPase subunits of the base, Rpt1-6 in yeast, and PSMC1 (Rpt2), PSMC2 (Rpt1), PSMC3 (Rpt4), PSMC4 (Rpt6), PSMC5 (Rpt3) and PSMC6 (Rpt5) in human 19S RP, are required not only for substrate unfolding using energy released by ATP hydrolysis, but also for a ring channel opening in the 20S core particle (20S CP). The order of the base precursor assembly has not been fully elucidated. PAAF1, PSMD10, and PSMD2 can be found bound to the fully assembled 19S regulatory particle (19S RP) but not to the 26S proteasome, suggesting that they are normally released prior to or during 19S RP binding to the 20S core particle (20S CP) (reviewed in Tomko and Hochstrasse 2013). Study of the assembly of human 19S RP base shows that the PSMD9 module is the last to incorporate during the base formation and that PSMD9 likely prevents premature association of the PSMC3:PSMC6 dimer with the base (Kaneko et al. 2009). The PSMC3:PSMC6 dimer is likely needed for the association of PSMD1 (Rpn2) with the base, and binding of PSMD1 to the base appears to be mutually exclusive with binding of PSMD9 (Kaneko et al. 2009). PSMD1 provides a docking site for ADRM1 (ortholog of yeast Rpn13) and enables recruitment of ADRM1, which serves as a ubiquitin receptor, to the proteasome base (Hamazaki et al. 2006; Chen et al. 2010; Lu et al. 2015; Lu et al. 2017; VanderLinden et al. 2017). The interaction between ADRM1 and PSMD1 may be regulated by PSMD1 SUMOylation (Ryu et al. 2014) and phosphorylation (Hemmis et al. 2019). |
| (summation) | [BlackBoxEvent:9907980] Formation of the 19S regulatory particle base precursor [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Following the formation of PSMD10:PSMC4:PSMC5:PAAF1, PSMD9:P... (9907989)
