ArticleProceedings of the National Academy of Sciences of the United States of America2015
Activation of the bacterial thermosensor DesK involves a serine zipper dimerization motif that is modulated by bilayer thickness.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 63 citations in OpenAlex.
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- Homeostatic regulation of intrinsic lipid curvature in eukaryotic cells.bioRxiv : the preprint server for biology · 2025Article
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- Allosteric coupling between a lipid bilayer and a membrane protein.Biophysical journal · 2025Article
- Allosteric coupling activation mechanism in histidine kinases.Scientific reports · 2025Article
- Quantification of membrane fluidity in bacteria using TIR-FCS.Biophysical journal · 2024Article
- Lipid phase separation impairs membrane thickness sensing by theMicrobiology spectrum · 2024Article
- Temperature-sensing riboceptors.RNA biology · 2024Article
- Membrane homeostasis beyond fluidity: control of membrane compressibility.Trends in biochemical sciences · 2023Review
- Regulation of membrane protein structure and function by their lipid nano-environment.Nature reviews. Molecular cell biology · 2023Review
- CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.Communications biology · 2022Article
- CPK28-NLP7 module integrates cold-induced CaScience advances · 2022Article
- Regulated strategies of cold-adapted microorganisms in response to cold: a review.Environmental science and pollution research international · 2021Review
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Article
- Bacterial cyclic diguanylate signaling networks sense temperature.Nature communications · 2021Article
- Driving the catalytic activity of a transmembrane thermosensor kinase.Cellular and molecular life sciences : CMLS · 2020Article
- Induction of Daptomycin Tolerance in Enterococcus faecalis by Fatty Acid Combinations.Applied and environmental microbiology · 2020Article
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Authors and funding
9 authors at 4 institutions in 4 countries.
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Abstract
DesK is a bacterial thermosensor protein involved in maintaining membrane fluidity in response to changes in environmental temperature. Most likely, the protein is activated by changes in membrane thickness, but the molecular mechanism of sensing and signaling is still poorly understood. Here we aimed to elucidate the mode of action of DesK by studying the so-called "minimal sensor DesK" (MS-DesK), in which sensing and signaling are captured in a single transmembrane segment. This simplified version of the sensor allows investigation of membrane thickness-dependent protein-lipid interactions simply by using synthetic peptides, corresponding to the membrane-spanning parts of functional and nonfunctional mutants of MS-DesK incorporated in lipid bilayers with varying thicknesses. The lipid-dependent behavior of the peptides was investigated by circular dichroism, tryptophan fluorescence, and molecular modeling. These experiments were complemented with in vivo functional studies on MS-DesK mutants. Based on the results, we constructed a model that suggests a new mechanism for sensing in which the protein is present as a dimer and responds to an increase in bilayer thickness by membrane incorporation of a C-terminal hydrophilic motif. This results in exposure of three serines on the same side of the transmembrane helices of MS-DesK, triggering a switching of the dimerization interface to allow the formation of a serine zipper. The final result is activation of the kinase state of MS-DesK.
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