ArticleThe Plant cell1994
The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals.
Article in The Plant cell, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 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.
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Who cites it
75 citing papers in PubMed, 213 citations in OpenAlex.
- Review
- Comparative Analysis of Dehydrins from Woody Plant Species.Biomolecules · 2024Article
- Article
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- Involvement of dehydrin proteins in mitigating the negative effects of drought stress in plants.Plant cell reports · 2022Review
- 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
- Expression, Purification, and Preliminary Protection Study of Dehydrin PicW1 From the Biomass ofFrontiers in bioengineering and biotechnology · 2022Article
- Comparative Genomics, Evolution, and Drought-Induced Expression of Dehydrin Genes in ModelPlants (Basel, Switzerland) · 2021Article
- Plant Dehydrins: Expression, Regulatory Networks, and Protective Roles in Plants Challenged by Abiotic Stress.International journal of molecular sciences · 2021Review
- Subcellular Proteomics to Understand Promotive Effect of Plant-Derived Smoke Solution on Soybean Root.Proteomes · 2021Article
- Effect of K-/S- segments on subcellular localization and dimerization of wheat dehydrin WZY1-2.Plant signaling & behavior · 2020Article
- Distribution and Classification of Dehydrins in Selected Plant Species Using Bioinformatics Approach.Iranian journal of biotechnology · 2020Article
- Epigenetic Regulation of ABA-Induced Transcriptional Responses in Maize.G3 (Bethesda, Md.) · 2020Article
- Lysine, Lysine-Rich, Serine, and Serine-Rich Proteins: Link Between Metabolism, Development, and Abiotic Stress Tolerance and the Role of ncRNAs in Their Regulation.Frontiers in plant science · 2020Review
- Article
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
- Functional characterization of KS-type dehydrin ZmDHN13 and its related conserved domains under oxidative stress.Scientific reports · 2017Article
- Multifunctional Roles of Plant Dehydrins in Response to Environmental Stresses.Frontiers in plant science · 2017Article
- Genome Analysis of Conserved Dehydrin Motifs in Vascular Plants.Frontiers in plant science · 2017Article
15 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
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maize abscisic acid (ABA)-responsive rab17 mRNA and Rab17 protein distribution in maize embryo tissues was investigated by in situ hybridization and immunocytochemistry. rab17 mRNA and Rab17 protein were found in all cells of embryo tissues. Synthesis of rab17 mRNA occurred initially in the embryo axis. As maturation progressed, rab17 mRNA was detectable in the scutellum and accumulated in axis cells and provascular tissues. However, the response to exogenous ABA differed in various embryo cell types. The Rab17 protein was located in the nucleus and in the cytoplasm, and qualitative differences in the phosphorylation states of the protein were found between the two subcellular compartments. Based on the similar domain arrangements of Rab17 and a nuclear localization signal (NLS) binding phosphoprotein, Nopp140, interaction of Rab17 with NLS peptides was studied. We found specific binding of Rab17 to the wild-type NLS of the SV40 T antigen but not to an import incompetent mutant peptide. Moreover, binding of the NLS peptide to Rab17 was found to be dependent upon phosphorylation. These results suggest that Rab17 may play a role in nuclear protein transport.
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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.