ArticleMolecular cell2015
A Phosphosignaling Adaptor Primes the AAA+ Protease ClpXP to Drive Cell Cycle-Regulated Proteolysis.
Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Disrupting NtrC function reveals unexpected robustness in a central cell cycle regulatory network.mBio · 2025Article
- MecA: A Multifunctional ClpP-Dependent and Independent Regulator in Gram-Positive Bacteria.Molecular microbiology · 2025Review
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- Proteolytic control of FixT by the Lon protease impacts FixLJ signaling inJournal of bacteriology · 2024Article
- ApoE Mimetic Peptide COG1410 KillsAntibiotics (Basel, Switzerland) · 2024Article
- ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation.Communications biology · 2023Article
- Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.Nature communications · 2023Article
- ATP hydrolysis tunes specificity of a AAA+ protease.Cell reports · 2022Article
- Review
- Targeting the Achilles' Heel of Multidrug-ResistantInternational journal of molecular sciences · 2022Article
- Proteolysis dependent cell cycle regulation in Caulobacter crescentus.Cell division · 2022Review
- Proteomic analysis of the regulatory networks of ClpX in a model cyanobacteriumFrontiers in plant science · 2022Article
- 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
- Construction of intracellular asymmetry and asymmetric division in Escherichia coli.Nature communications · 2021Article
- Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex.Nature communications · 2021Article
- The Protein Quality Control Network inFrontiers in molecular biosciences · 2021Review
- Programmed Proteolysis of Chemotaxis Proteins in Sinorhizobium meliloti: Features in the C-Terminal Region Control McpU Degradation.Journal of bacteriology · 2020Article
- The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Journal of molecular biology · 2020Article
- Multilayered control of chromosome replication inBiochemical Society transactions · 2019Review
- Polar Localization Hub Protein PopZ Restrains Adaptor-Dependent ClpXP Proteolysis in Caulobacter crescentus.Journal of bacteriology · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The response regulator CpdR couples phosphorylation events in Caulobacter crescentus with the AAA+ protease ClpXP to provide punctuated degradation of crucial substrates involved in cell cycle regulation. CpdR functions like an adaptor to alter substrate choice by ClpXP; however, it remains unclear how CpdR influences its multiple targets. Here we show that, unlike canonical ClpXP adaptors, CpdR alone does not strongly bind its substrate. Instead, CpdR binds the N-terminal domain of ClpX and prepares (primes) the unfoldase for substrate engagement. This priming creates a recruitment interface that docks multiple substrates and additional adaptor components. We show that adaptor-dependent priming of ClpX avoids concentration-dependent inhibition that limits traditional scaffolding adaptors. Phosphosignaling disrupts the adaptor-protease interaction, and mutations in CpdR that impact ClpX binding tune adaptor activity and biological function. Together, these results reveal how a single adaptor can command global changes in proteome composition through priming of a protease.
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