ArticlePlant physiology2016
Membrane-Induced Folding of the Plant Stress Dehydrin Lti30.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 60 citations in OpenAlex.
- Hyperactive ice-binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans.FEBS open bio · 2026Article
- Molecular timekeepers: the curious alliance of redox, repair, and protective proteins in preserving seed longevity.Crop health · 2026Review
- Environmental Factors, Developmental Genes and Oxidative Stress Determine Inter-Species Variability in Seed Longevity in Salicaceae.Plants (Basel, Switzerland) · 2025Article
- Order in Chaos: Lesser-Conserved and Repeat Structures in Dehydrins.Biomolecules · 2025Article
- Overexpression of soybeanGM crops & food · 2024Article
- New Insights into Involvement of Low Molecular Weight Proteins in Complex Defense Mechanisms in Higher Plants.International journal of molecular sciences · 2024Review
- Genome-wide characterization of LEA gene family reveals a positive role of BnaA.LEA6.a in freezing tolerance in rapeseed (Brassica napus L.).BMC plant biology · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Research progress on the physiological response and molecular mechanism of cold response in plants.Frontiers in plant science · 2024Review
- Dynamic conformational changes of a tardigrade group-3 late embryogenesis abundant protein modulate membrane biophysical properties.PNAS nexus · 2024Article
- Dehydrin CaDHN2 Enhances Drought Tolerance by Affecting Ascorbic Acid Synthesis under Drought in Peppers.Plants (Basel, Switzerland) · 2023Article
- Bioinformatic and functional analysis of OsDHN2 under cadmium stress.Functional & integrative genomics · 2023Article
- Plant dehydrins and dehydrin-like proteins: characterization and participation in abiotic stress response.Frontiers in plant science · 2023Review
- Novel molecules and target genes for vegetative heat tolerance in wheat.Plant-environment interactions (Hoboken, N.J.) · 2022Article
- The Halophyte Dehydrin Sequence Landscape.Biomolecules · 2022Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins.Frontiers in plant science · 2022Review
- Evolutionary analysis of angiosperm dehydrin gene family reveals three orthologues groups associated to specific protein domains.Scientific reports · 2021Article
- Plant Dehydrins: Expression, Regulatory Networks, and Protective Roles in Plants Challenged by Abiotic Stress.International journal of molecular sciences · 2021Review
- Functional Characteristics Analysis of Dehydrins inInternational journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydrins are disordered proteins that are expressed in plants as a response to embryogenesis and water-related stress. The molecular function and structural action of the dehydrins are yet elusive, but increasing evidence points to a role in protecting the structure and functional dynamics of cell membranes. An intriguing example is the cold-induced dehydrin Lti30 that binds to membranes by its conserved K segments. Moreover, this binding can be regulated by pH and phosphorylation and shifts the membrane phase transition to lower temperatures, consistent with the protein's postulated function in cold stress. In this study, we reveal how the Lti30-membrane interplay works structurally at atomic level resolution in Arabidopsis (Arabidopsis thaliana). Nuclear magnetic resonance analysis suggests that negatively charged lipid head groups electrostatically capture the protein's disordered K segments, which locally fold up into α-helical segments on the membrane surface. Thus, Lti30 conforms to the general theme of structure-function relationships by folding upon binding, in spite of its disordered, atypically hydrophilic and repetitive sequence signatures. Moreover, the fixed and well-defined structure of the membrane-bound K segments suggests that dehydrins have the molecular prerequisites for higher level binding specificity and regulation, raising new questions about the complexity of their biological function.
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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.