ArticleStructure (London, England : 1993)2012
Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 29 citations in OpenAlex.
- Global analysis of protein degradation reveals instability of diverse regulators inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- An open axial channel of the AAA ClpXP protease enhances degradation of specific classes of protein substrates.Protein science : a publication of the Protein Society · 2026Article
- The HmrABCX pathway regulates the transition between motile and sessile lifestyles inbioRxiv : the preprint server for biology · 2023Article
- Cargo competition for a dimerization interface restricts and stabilizes a bacterial protease adaptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Article
- Polar Localization Hub Protein PopZ Restrains Adaptor-Dependent ClpXP Proteolysis in Caulobacter crescentus.Journal of bacteriology · 2018Article
- The Essential Role of ClpXP inFrontiers in molecular biosciences · 2017Article
- Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016Review
- An intracellular compass spatially coordinates cell cycle modules in Caulobacter crescentus.Current opinion in microbiology · 2016Review
- Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Nature reviews. Microbiology · 2016Review
- Article
- Rapid pairing and resegregation of distant homologous loci enables double-strand break repair in bacteria.The Journal of cell biology · 2015Article
- A Phosphosignaling Adaptor Primes the AAA+ Protease ClpXP to Drive Cell Cycle-Regulated Proteolysis.Molecular cell · 2015Article
- Sinorhizobium meliloti CtrA Stability Is Regulated in a CbrA-Dependent Manner That Is Influenced by CpdR1.Journal of bacteriology · 2015Article
- A cell cycle-controlled redox switch regulates the topoisomerase IV activity.Genes & development · 2015Article
- ClpXP and ClpAP proteolytic activity on divisome substrates is differentially regulated following the Caulobacter asymmetric cell division.Molecular microbiology · 2014Article
- Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014Review
- Critical clamp loader processing by an essential AAA+ protease in Caulobacter crescentus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development.Molecular microbiology · 2013Article
Corrections and comments
- Commented on by
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In Caulobacter crescentus, the ClpXP protease degrades several crucial cell-cycle regulators, including the phosphodiesterase PdeA. Degradation of PdeA requires the response regulator CpdR and signals a morphological transition in concert with initiation of DNA replication. Here, we report the structure of a Per-Arnt-Sim (PAS) domain of PdeA and show that it is necessary for CpdR-dependent degradation in vivo and in vitro. CpdR acts as an adaptor, tethering the amino-terminal PAS domain to ClpXP and promoting recognition of the weak carboxyl-terminal degron of PdeA, a combination that ensures processive proteolysis. We identify sites on the PAS domain needed for CpdR recognition and find that one subunit of the PdeA dimer can be delivered to ClpXP by its partner. Finally, we show that improper stabilization of PdeA in vivo alters cellular behavior. These results introduce an adaptor/substrate pair for ClpXP and reveal broad diversity in adaptor-mediated proteolysis.
Indexed as
Identifiers
What OpenQuestion holds
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.