ArticleThe Plant cell2004
Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database.
Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.
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Who cites it
175 citing papers in PubMed, 476 citations in OpenAlex.
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- EPSD 2.0: An Updated Database of Protein Phosphorylation Sites Across Eukaryotic Species.Genomics, proteomics & bioinformatics · 2025Article
- Population sequencing of cherry accessions unravels the evolution of Cerasus species and the selection of genetic characteristics in edible cherries.Molecular horticulture · 2025Article
- MicroRNAs as potent regulators in nitrogen and phosphorus signaling transduction and their applications.Stress biology · 2024Review
- Regulation of developmental gatekeeping and cell fate transition by the calpain protease DEK1 in Physcomitrium patens.Communications biology · 2024Article
- Assaying the Effect of Peptide Treatment on HMethods in molecular biology (Clifton, N.J.) · 2024Article
- Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation.Plant communications · 2023Article
- Ammonium Uptake, Mediated by Ammonium Transporters, Mitigates Manganese Toxicity in Duckweed,Plants (Basel, Switzerland) · 2023Article
- Membrane-anchored calpains - hidden regulators of growth and development beyond plants?Frontiers in plant science · 2023Article
- Abscisic acid influences ammonium transport via regulation of kinase CIPK23 and ammonium transporters.Plant physiology · 2022Article
- The functions of phospholipases and their hydrolysis products in plant growth, development and stress responses.Progress in lipid research · 2022Review
- The Genetic Basis of Phosphorus Utilization Efficiency in Plants Provide New Insight into Woody Perennial Plants Improvement.International journal of molecular sciences · 2022Review
- Emerging role of phospholipase C mediated lipid signaling in abiotic stress tolerance and development in plants.Plant cell reports · 2021Review
- Posttranslational Modifications: Regulation of Nitrogen Utilization and Signaling.Plant & cell physiology · 2021Review
- Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Lipid flippases as key players in plant adaptation to their environment.Nature plants · 2021Review
- Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Membrane Profiling by Free Flow Electrophoresis and SWATH-MS to Characterize Subcellular Compartment Proteomes inInternational journal of molecular sciences · 2021Article
- Nitrogen Uptake in Plants: The Plasma Membrane Root Transport Systems from a Physiological and Proteomic Perspective.Plants (Basel, Switzerland) · 2021Review
115 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional genomic technologies are generating vast amounts of data describing the presence of transcripts or proteins in plant cells. Together with classical genetics, these approaches broaden our understanding of the gene products required for specific responses. Looking to the future, the focus of research must shift to the dynamic aspects of biology: molecular mechanisms of function and regulation. Phosphorylation is a key regulatory factor in all aspects of plant biology; but it is difficult, if not impossible, for most researchers to identify in vivo phosphorylation sites within their proteins of interest. We have developed a large-scale strategy for the isolation of phosphopeptides and identification by mass spectrometry (Nühse et al., 2003b). Here, we describe the identification of more than 300 phosphorylation sites from Arabidopsis thaliana plasma membrane proteins. These data will be a valuable resource for many fields of plant biology and overcome a major impediment to the elucidation of signal transduction pathways. We present an analysis of the characteristics of phosphorylation sites, their conservation among orthologs and paralogs, and the existence of putative motifs surrounding the sites. These analyses yield general principles for predicting other phosphorylation sites in plants and provide indications of specificity determinants for responsible kinases. In addition, more than 50 sites were mapped on receptor-like kinases and revealed an unexpected complexity of regulation. Finally, the data also provide empirical evidence on the topology of transmembrane proteins. This information indicates that prediction programs incorrectly identified the cytosolic portion of the protein in 25% of the transmembrane proteins found in this study. All data are deposited in a new searchable database for plant phosphorylation sites maintained by PlantsP (http://plantsp.sdsc.edu) that will be updated as the project expands to encompass additional tissues and organelles.
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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.