ArticlePlant physiology1993
Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L.
Article in Plant physiology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
The trial behind it
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Who cites it
18 citing papers in PubMed, 60 citations in OpenAlex.
- The localization of phototropin to the plasma membrane defines a cold-sensing compartment inPNAS nexus · 2022Article
- Comparative transcriptome profiling and weighted gene co-expression network analysis to identify core genes in maize (Frontiers in plant science · 2022Article
- Relationship between relocation of phototropin to the chloroplast periphery and the initiation of chloroplast movement inPlant direct · 2019Article
- Blue Light-Induced Intracellular Movement of Phototropins: Functional Relevance or Red Herring?Frontiers in plant science · 2016Article
- Phytochrome A Mediates Blue-Light Enhancement of Second-Positive Phototropism in Arabidopsis.Frontiers in plant science · 2016Article
- Light-harvesting regulation from leaf to molecule with the emphasis on rapid changes in antenna size.Photosynthesis research · 2015Review
- The Arabidopsis rcn1-1 mutation impairs dephosphorylation of Phot2, resulting in enhanced blue light responses.The Plant cell · 2010Article
- Secret message at the plant surface.Plant signaling & behavior · 2007Article
- Article
- Tissue-specific and subcellular localization of phototropin determined by immuno-blotting.Planta · 2004Article
- Primary inhibition of hypocotyl growth and phototropism depend differently on phototropin-mediated increases in cytoplasmic calcium induced by blue light.Plant physiology · 2003Article
- Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean.Plant physiology · 2003Article
- Cellular and subcellular localization of phototropin 1.The Plant cell · 2002Article
- Exposure of oat seedlings to blue light results in amplified phosphorylation of the putative photoreceptor for phototropism and in higher sensitivity of the plants to phototropic stimulation.Plant physiology · 1997Article
- Changes in blue-light-dependent protein phosphorylation during the early development of etiolated oat seedlings.Planta · 1996Article
- Article
- Blue Light Induces Phosphorylation at Seryl Residues on a Pea (Pisum sativum L.) Plasma Membrane Protein.Plant physiology · 1994Article
- Correlation of Blue Light-Induced Phosphorylation to Phototropism in Zea mays L.Plant physiology · 1993Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fluence levels that are sufficient to stimulate phototropic curvature. Phosphorylation in response to blue light can be detected in vivo in coleoptile tips preincubated in 32Pi or in vitro in isolated membranes supplemented with [[gamma]-32P]ATP. Phosphorylation reaches a maximum level in vitro within 2 min following an inductive light pulse, but substantial labeling occurs within the first 15 s. Isolated membranes remain activated for several minutes following an in vitro blue light stimulus, even in the absence of exogenous ATP. Phosphoamino acid analysis of the 114-kD protein detected phosphoserine and a trace of phosphothreonine. The kinase involved in phosphorylating the protein in vitro is not dependent on calcium. The 114-kD protein itself has an apparent binding site for ATP, detected by incubating with the nonhydrolyzable analog, 5[prime]-p-fluorosulfonyl-benzoyladenosine. This result suggests that the 114-kD protein, which becomes phosphorylated in response to blue light, may also be capable of kinase activity.
Identifiers
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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.