ArticleThe Journal of biological chemistry2013
ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- PI31 is a positive regulator of 20S immunoproteasome assembly.Journal of cell science · 2025Article
- An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation.eLife · 2022Article
- Association with proteasome determines pathogenic threshold of polyglutamine expansion diseases.Biochemical and biophysical research communications · 2021Article
- Proteasome dysfunction in alveolar type 2 epithelial cells is associated with acute respiratory distress syndrome.Scientific reports · 2019Article
- Identification of Carassius auratus gibelio liver cell proteins interacting with the GABAFish physiology and biochemistry · 2019Article
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
- Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.Frontiers in molecular biosciences · 2019Review
- Substrate-engaged 26Science (New York, N.Y.) · 2018Article
- ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.Cell reports · 2018Article
- FOXOs modulate proteasome activity in human-induced pluripotent stem cells of Huntington's disease and their derived neural cells.Human molecular genetics · 2017Article
- Phosphatase UBLCP1 controls proteasome assembly.Open biology · 2017Article
- Article
- Tuning the proteasome to brighten the end of the journey.American journal of physiology. Cell physiology · 2016Review
- ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.Nature communications · 2015Article
- Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly.Scientific reports · 2015Article
- N-Terminal Coiled-Coil Structure of ATPase Subunits of 26S Proteasome Is Crucial for Proteasome Function.PloS one · 2015Article
- Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function.The Journal of biological chemistry · 2014Article
- Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Regulated protein turnover: snapshots of the proteasome in action.Nature reviews. Molecular cell biology · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We examined the role of ATP binding by six different ATPase subunits (Rpt1-6) in the cellular assembly and molecular functions of mammalian 26 S proteasome. Four Rpt subunits (Rpt1-4) with ATP binding mutations were incompetent for cellular assembly into 26 S proteasome. In contrast, analogous mutants of Rpt5 and Rpt6 were incorporated normally into 26 S proteasomes in both intact cells and an in vitro assembly assay. Surprisingly, purified 26 S proteasomes containing either mutant Rpt5 or Rpt6 had normal basal ATPase activity and substrate gate opening for hydrolysis of short peptides. However, these mutant 26 S proteasomes were severely defective for ATP-dependent in vitro degradation of ubiquitylated and non-ubiquitylated proteins and did not display substrate-stimulated ATPase and peptidase activities characteristic of normal proteasomes. These results reveal differential roles of ATP binding by various Rpt subunits in proteasome assembly and function. They also indicate that substrate-stimulated ATPase activity and gating depend on the concerted action of a full complement of Rpt subunits competent for ATP binding and that this regulation is essential for normal proteolysis. Thus, protein substrates appear to promote their own degradation by stimulating proteasome functions involved in proteolysis.
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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.