ArticleBiomolecules2019
In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Mapping Interaction of Assembly Factor Rpn14 With the Proteasome Base Reveals a Bipartite Interface and Implies Ordered Remodeling of Intersubunit Contacts During Proteasome Biogenesis.Journal of molecular biology · 2026Article
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Molecular mechanisms in rare proteasomopathies.EULAR rheumatology open · 2026Review
- Hepatitis B virus infection disrupts homologous recombination in hepatocellular carcinoma by stabilizing resection inhibitor ADRM1.The Journal of clinical investigation · 2023Article
- Fungal COP9 signalosome assembly requires connection of two trimeric intermediates for integration of intrinsic deneddylase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis.Biomolecules · 2023Review
- The RPN12a proteasome subunit is essential for the multiple hormonal homeostasis controlling the progression of leaf senescence.Communications biology · 2022Article
- Proteasomal subunit depletions differentially affect germline integrity inFrontiers in cell and developmental biology · 2022Article
- Protective Roles of Cytosolic and Plastidal Proteasomes on Abiotic Stress and Pathogen Invasion.Plants (Basel, Switzerland) · 2020Review
- Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 26S proteasome is a key player in the degradation of ubiquitinated proteins, comprising a 20S core particle (CP) and a 19S regulatory particle (RP). The RP is further divided into base and lid subcomplexes, which are assembled independently from each other. We have previously demonstrated the assembly pathway of the CP and the base by observing assembly intermediates resulting from knockdowns of each proteasome subunit and the assembly chaperones. In this study, we examine the assembly pathway of the mammalian lid, which remains to be elucidated. We show that the lid assembly pathway is conserved between humans and yeast. The final step is the incorporation of Rpn12 into the assembly intermediate consisting of two modular complexes, Rpn3-7-15 and Rpn5-6-8-9-11, in both humans and yeast. Furthermore, we dissect the assembly pathways of the two modular complexes by the knockdown of each lid subunit.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.