ArticlePlanta2005
LeRALF, a plant peptide that regulates root growth and development, specifically binds to 25 and 120 kDa cell surface membrane proteins of Lycopersicon peruvianum.
Article in Planta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Peptide hormones in plants.Molecular horticulture · 2025Review
- FERONIA: A Receptor Kinase at the Core of a Global Signaling Network.Annual review of plant biology · 2024Review
- TheInternational journal of molecular sciences · 2023Article
- Twenty Years of Progress in Physiological and Biochemical Investigation of RALF Peptides.Plant physiology · 2020Review
- Perception of Damaged Self in Plants.Plant physiology · 2020Review
- Article
- BAK1 is involved in AtRALF1-induced inhibition of root cell expansion.PLoS genetics · 2017Article
- Expansion and evolutionary patterns of cysteine-rich peptides in plants.BMC genomics · 2017Article
- Novel disease susceptibility factors for fungal necrotrophic pathogens in Arabidopsis.PLoS pathogens · 2015Article
- Arabidopsis thaliana RALF1 opposes brassinosteroid effects on root cell elongation and lateral root formation.Journal of experimental botany · 2014Article
- Isolation and characterization of a novel BcMF14 gene from Brassica campestris ssp. chinensis.Molecular biology reports · 2011Article
- RALFs: peptide regulators of plant growth.Plant signaling & behavior · 2010Review
- Cloning and expression analysis of a pollen preferential rapid alkalinization factor gene, BoRALF1, from broccoli flowers.Molecular biology reports · 2010Article
- A pollen-specific RALF from tomato that regulates pollen tube elongation.Plant physiology · 2010Article
- SacRALF1, a peptide signal from the grass sugarcane (Saccharum spp.), is potentially involved in the regulation of tissue expansion.Plant molecular biology · 2010Article
- STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro.BMC plant biology · 2010Article
- Synthetic ultrashort cationic lipopeptides induce systemic plant defense responses against bacterial and fungal pathogens.Applied and environmental microbiology · 2009Article
- Genomic expression profiling of mature soybean (Glycine max) pollen.BMC plant biology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A photoaffinity analog of tomato leaf RALF peptide (LeRALF), (125)I-azido-LeRALF, bound saturably to tomato suspension cultured cells in the dark in a classical receptor binding assay. Classical kinetic analyses revealed that the analog interacted with a single binding site on the surface of the cells with a KD of 0.8x10(-9) M, typical of known peptide hormone-receptor interactions in both plants and animals. The (125)I-azido-LeRALF, when exposed to UVB light in the presence of the cells, strongly labeled only two proteins of 25 kDa and 120 kDa, with the 25 kDa protein being more strongly labeled than the 120 kDa protein. The cell-surface localization of the interaction was indicated, as suramin, a known inhibitor of peptide-receptor interactions, and native LeRALF peptide competed with (125)I-azido-LeRALF labeling of both proteins. Two biologically inactive LeRALF analogs were not competitors. Incubation of (125)I-azido-LeRALF with suspension cultured cells in the dark, where it was fully active, could subsequently be totally dissociated from cells by acid washes, indicating that it was interacting at the cell surface and was not internalized. The (125)I-azido-LeRALF-labeled 25 kDa and 120 kDa proteins could not be solubilized from cell membranes by methods that release peripheral proteins, indicating that they are integral membrane components. The cumulative kinetic and biochemical evidence strongly indicates that the two proteins may be components of a LeRALF receptor complex.
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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.