ArticleThe Plant cell2014
The ubiquitous distribution of late embryogenesis abundant proteins across cell compartments in Arabidopsis offers tailored protection against abiotic stress.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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Who cites it
122 citing papers in PubMed.
- A phosphatidic acid-based retrograde signaling pathway responsive to abiotic stress in Arabidopsis.The Plant journal : for cell and molecular biology · 2026Article
- Engineering climate-resilient horticultural crops: advances in transcriptional regulation, genome editing, and synthetic networks.Horticulture research · 2026Article
- Loss of ASMT Function in Arabidopsis Affects Hormone Pathways and the Ability to Withstand Drought Stress.International journal of molecular sciences · 2026Article
- Hyperactive ice-binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans.FEBS open bio · 2026Article
- A chromosome-scale genome assembly of Hordeum erectifolium: genomic, transcriptomic and anatomical adaptations to drought in a wild barley relative.The New phytologist · 2026Article
- Molecular timekeepers: the curious alliance of redox, repair, and protective proteins in preserving seed longevity.Crop health · 2026Review
- A multi-locus genome-wide association study uncovers candidate genes for alkali tolerance in maize (Zea Mays L.) seedlings.BMC genomics · 2025Article
- Genome-wide identification, structural characterization and gene expression analysis of the LEA_2 gene family in faba bean (Vicia Faba L.).BMC plant biology · 2025Article
- Genome-Wide Analysis of theBiology · 2025Article
- Structural flexibility of a recombinant intrinsically disordered LEA protein from Ramonda serbica.Scientific reports · 2025Article
- Stress Regulatory capabilities discovered in late embryogenesis abundant (LEA) proteins expressed during pecan (Carya illinoinensis) kernel development.BMC genomics · 2025Article
- Genome-Wide Identification of theGenes · 2025Article
- The transcription factor ClWRKY61 interacts with ClLEA55 to enhance salt tolerance in watermelon.Horticulture research · 2025Article
- ACT2.6: Global Gene Coexpression Network inGenes · 2025Article
- What Happens Inside the Germinating Grain After Microbial Decontamination by Pulsed Electric Field? Data-Driven Multi-Omics Helps Find the Answer.Molecules (Basel, Switzerland) · 2025Article
- Article
- Genome-Wide Identification, Phylogenetic Evolution, and Abiotic Stress Response Analyses of the Late Embryogenesis Abundant Gene Family in the Alpine Cold-Tolerant MedicinalInternational journal of molecular sciences · 2025Article
- Overexpression ofPlants (Basel, Switzerland) · 2025Article
- LEA proteins and ABA signaling: reciprocal regulation in stress adaptation.Frontiers in plant science · 2025Review
- Towards resilience: Transcriptional insights on flavonoid biosynthesis during peanut seed maturation phases.PloS one · 2025Article
62 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Late embryogenesis abundant (LEA) proteins are hydrophilic, mostly intrinsically disordered proteins, which play major roles in desiccation tolerance. In Arabidopsis thaliana, 51 genes encoding LEA proteins clustered into nine families have been inventoried. To increase our understanding of the yet enigmatic functions of these gene families, we report the subcellular location of each protein. Experimental data highlight the limits of in silico predictions for analysis of subcellular localization. Thirty-six LEA proteins localized to the cytosol, with most being able to diffuse into the nucleus. Three proteins were exclusively localized in plastids or mitochondria, while two others were found dually targeted to these organelles. Targeting cleavage sites could be determined for five of these proteins. Three proteins were found to be endoplasmic reticulum (ER) residents, two were vacuolar, and two were secreted. A single protein was identified in pexophagosomes. While most LEA protein families have a unique subcellular localization, members of the LEA_4 family are widely distributed (cytosol, mitochondria, plastid, ER, and pexophagosome) but share the presence of the class A α-helix motif. They are thus expected to establish interactions with various cellular membranes under stress conditions. The broad subcellular distribution of LEA proteins highlights the requirement for each cellular compartment to be provided with protective mechanisms to cope with desiccation or cold stress.
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