ReviewCurrent opinion in microbiology2015
Ser/Thr phosphorylation as a regulatory mechanism in bacteria.
Review in Current opinion in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
What it found
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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.
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Who cites it
74 citing papers in PubMed, 130 citations in OpenAlex.
- Phosphorylation of a novel STK substrate SstP1 links SUF Fe-S cluster biogenesis to oxidative stress resistance and virulence inVirulence · 2026Article
- Roles of PknB and CslA in Cell Wall Morphogenesis of Streptomyces.Molecular microbiology · 2026Article
- Serine/threonine protein kinase phosphorylation of DosR alters target gene transcription mechanics and regulates Mycobacterium tuberculosis response to nitric oxide stress.PLoS genetics · 2026Article
- Multiple input-multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis.FEMS microbiology reviews · 2026Review
- Phosphorylation of a conserved intrinsically disordered region is necessary for activation of a bacterial Hanks-type Ser/Thr kinase signaling pathway.bioRxiv : the preprint server for biology · 2025Article
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution.PloS one · 2025Article
- Experimental measurement and computational prediction of bacterial Hanks-type Ser/Thr signaling system regulatory targets.Molecular microbiology · 2024Review
- Article
- Review
- Regulatory Intersection of Two-component System and Ser/Thr Protein Kinase Signaling in Mycobacterium tuberculosis.Journal of molecular biology · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Maintenance of heme homeostasis inJournal of bacteriology · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Shining a light on bacterial environmental cue integration and its relation to metabolism.Molecular microbiology · 2023Article
- The Mycobacterium tuberculosis protein O-phosphorylation landscape.Nature microbiology · 2023Article
- A Novel Capsule Network with Attention Routing to Identify Prokaryote Phosphorylation Sites.Biomolecules · 2022Article
- Positive selection-driven fixation of a hominin-specific amino acid mutation related to dephosphorylation in IRF9.BMC ecology and evolution · 2022Article
- Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis.PLoS pathogens · 2022Article
- PrrA modulates Mycobacterium tuberculosis response to multiple environmental cues and is critically regulated by serine/threonine protein kinases.PLoS genetics · 2022Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
This review will discuss some recent work describing the role of Ser/Thr phosphorylation as a post-translational mechanism of regulation in bacteria. I will discuss the interaction between bacterial eukaryotic-like Ser/Thr kinases (eSTKs) and two-component systems as well as hints as to physiological function of eSTKs and their cognate eukaryotic-like phosphatases (eSTPs). In particular, I will highlight the role of eSTKs and eSTPs in the regulation of peptidoglycan metabolism and protein synthesis. In addition, I will discuss how data from phosphoproteomic surveys suggest that Ser/Thr phosphorylation plays a much more significant physiological role than would be predicted simply based on in vivo and in vitro analyses of individual kinases.
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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.