ArticlePlant physiology1994
Blue Light Induces Phosphorylation at Seryl Residues on a Pea (Pisum sativum L.) Plasma Membrane Protein.
Article in Plant physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 31 citations in OpenAlex.
- The role of a 14-3-3 protein in stomatal opening mediated by PHOT2 in Arabidopsis.The Plant cell · 2012Article
- The Arabidopsis rcn1-1 mutation impairs dephosphorylation of Phot2, resulting in enhanced blue light responses.The Plant cell · 2010Article
- Possible involvement of phototropins in leaf movement of kidney bean in response to blue light.Plant physiology · 2005Article
- Tissue-specific and subcellular localization of phototropin determined by immuno-blotting.Planta · 2004Article
- Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean.Plant physiology · 2003Article
- Asymmetric, blue light-dependent phosphorylation of a 116-kilodalton plasma membrane protein can be correlated with the first- and second-positive phototropic curvature of oat coleoptiles.Plant physiology · 1997Article
- Changes in blue-light-dependent protein phosphorylation during the early development of etiolated oat seedlings.Planta · 1996Article
- Article
- Genes involved in light control of sexual differentiation in Chlamydomonas reinhardtii.Genetics · 1995Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have partially characterized the blue-light-stimulated in vitro phosphorylation of a membrane protein from etiolated Pisum sativum L. stems. Properties of the response have implicated its involvement in signal transduction of phototropic stimuli (T.W. Short, W.R. Briggs [1990] Plant Physiol 92: 179-185; P. Reymond, T.W. Short, W.R. Briggs [1992] Proc Natl Acad Sci USA 89: 4718- 4721). Analysis of proteolysis products and phosphoamino acidanalysis indicate that the substrate protein is phosphorylated on multiple seryl residues. Kinetics of the in vitro reaction show phosphorylation to be complete within 2 to 5 min at 30[deg]C in either light-exposed or dark-control plasma membrane preparations, regardless of whether the membranes were first solubilized in Triton X-100. Nucleotide competition assays show the kinase to be ATP specific. The pH optimum covers a broad range with a maximum near 7.5. A wide array of salts inhibits the phosphorylation at high concentrations, but millimolar concentrations of Mg2+ are required to form Mg.ATP complexes for maximal activity, whereas excess free Mg2+ or Ca2+ are not required for the reaction.
Identifiers
What OpenQuestion holds
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.