ArticleThe Journal of biological chemistry2012
Stable incorporation of ATPase subunits into 19 S regulatory particle of human proteasome requires nucleotide binding and C-terminal tails.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Role of the Ubiquitin System in Eye Diseases.Life (Basel, Switzerland) · 2025Review
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
- Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.Cell reports · 2018Article
- Phosphatase UBLCP1 controls proteasome assembly.Open biology · 2017Article
- Nucleotide-dependent switch in proteasome assembly mediated by the Nas6 chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis for dynamic regulation of the human 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The ubiquitin proteasomal system: a potential target for the management of Alzheimer's disease.Journal of cellular and molecular medicine · 2016Review
- Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly.Scientific reports · 2015Article
- Alpha-ring Independent Assembly of the 20S Proteasome.Scientific reports · 2015Article
- The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome.The Journal of biological chemistry · 2013Article
- Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase.Nature structural & molecular biology · 2013Article
- ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome.The Journal of biological chemistry · 2013Article
- Molecular architecture and assembly of the eukaryotic proteasome.Annual review of biochemistry · 2013Review
- Near-atomic resolution structural model of the yeast 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Genetic analyses of the Arabidopsis 26S proteasome regulatory particle reveal its importance during light stress and a specific role for the N-terminus of RPT2 in development.Plant signaling & behavior · 2012Article
- Functional asymmetries of proteasome translocase pore.The Journal of biological chemistry · 2012Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 26 S proteasome is a large multi-subunit protein complex that degrades ubiquitinated proteins in eukaryotic cells. Proteasome assembly is a complex process that involves formation of six- and seven-membered ring structures from homologous subunits. Here we report that the assembly of hexameric Rpt ring of the 19 S regulatory particle (RP) requires nucleotide binding but not ATP hydrolysis. Disruption of nucleotide binding to an Rpt subunit by mutation in the Walker A motif inhibits the assembly of the Rpt ring without affecting heterodimer formation with its partner Rpt subunit. Coexpression of the base assembly chaperones S5b and PAAF1 with mutant Rpt1 and Rpt6, respectively, relieves assembly inhibition of mutant Rpts by facilitating their interaction with adjacent Rpt dimers. The mutation in the Walker B motif which impairs ATP hydrolysis does not affect Rpt ring formation. Incorporation of a Walker B mutant Rpt subunit abrogates the ATPase activity of the 19 S RP, suggesting that failure of the mutant Rpt to undergo the conformational transition from an ATP-bound to an ADP-bound state impairs conformational changes in the other five wild-type Rpts in the Rpt ring. In addition, we demonstrate that the C-terminal tails of Rpt subunits possessing core particle (CP)-binding affinities facilitate the cellular assembly of the 19 S RP, implying that the 20 S CP may function as a template for base assembly in human cells. Taken together, these results suggest that the ATP-bound conformational state of an Rpt subunit with the exposed C-terminal tail is competent for cellular proteasome assembly.
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