ArticleThe Plant cell2011
Tunable membrane binding of the intrinsically disordered dehydrin Lti30, a cold-induced plant stress protein.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 159 citations in OpenAlex.
- From Shared Mechanisms to Precision Breeding: Engineering Cold and Drought Cross-Tolerance in Crops.International journal of molecular sciences · 2026Review
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Order in Chaos: Lesser-Conserved and Repeat Structures in Dehydrins.Biomolecules · 2025Article
- Altering cold-regulated gene expression decouples the salicylic acid-growth trade-off in Arabidopsis.The Plant cell · 2024Article
- The MsDHN1-MsPIP2;1-MsmMYB module orchestrates the trade-off between growth and survival of alfalfa in response to drought stress.Plant biotechnology journal · 2024Article
- Comparative Analysis of Dehydrins from Woody Plant Species.Biomolecules · 2024Article
- Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Dynamic conformational changes of a tardigrade group-3 late embryogenesis abundant protein modulate membrane biophysical properties.PNAS nexus · 2024Article
- Photosynthesis regulation, cell membrane stabilization and methylglyoxal detoxification seems major altered pathways under cold stress as revealed by integrated multi-omics meta-analysis.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Article
- Plant dehydrins and dehydrin-like proteins: characterization and participation in abiotic stress response.Frontiers in plant science · 2023Review
- Overexpression ofInternational journal of molecular sciences · 2022Article
- Article
- Involvement of dehydrin proteins in mitigating the negative effects of drought stress in plants.Plant cell reports · 2022Review
- Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- Expression, Purification, and Preliminary Protection Study of Dehydrin PicW1 From the Biomass ofFrontiers in bioengineering and biotechnology · 2022Article
- Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status.Frontiers in plant science · 2022Article
- Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins.Frontiers in plant science · 2022Review
- Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydrins are intrinsically disordered plant proteins whose expression is upregulated under conditions of desiccation and cold stress. Their molecular function in ensuring plant survival is not yet known, but several studies suggest their involvement in membrane stabilization. The dehydrins are characterized by a broad repertoire of conserved and repetitive sequences, out of which the archetypical K-segment has been implicated in membrane binding. To elucidate the molecular mechanism of these K-segments, we examined the interaction between lipid membranes and a dehydrin with a basic functional sequence composition: Lti30, comprising only K-segments. Our results show that Lti30 interacts electrostatically with vesicles of both zwitterionic (phosphatidyl choline) and negatively charged phospholipids (phosphatidyl glycerol, phosphatidyl serine, and phosphatidic acid) with a stronger binding to membranes with high negative surface potential. The membrane interaction lowers the temperature of the main lipid phase transition, consistent with Lti30's proposed role in cold tolerance. Moreover, the membrane binding promotes the assembly of lipid vesicles into large and easily distinguishable aggregates. Using these aggregates as binding markers, we identify three factors that regulate the lipid interaction of Lti30 in vitro: (1) a pH dependent His on/off switch, (2) phosphorylation by protein kinase C, and (3) reversal of membrane binding by proteolytic digest.
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