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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Key Elements for Plant Nutrition02:35

Key Elements for Plant Nutrition

Like all living organisms, plants require organic and inorganic nutrients to survive, reproduce, grow and maintain homeostasis. To identify nutrients that are essential for plant functioning, researchers have leveraged a technique called hydroponics. In hydroponic culture systems, plants are grown—without soil—in water-based solutions containing nutrients. At least 17 nutrients have been identified as essential elements required by plants. Plants acquire these elements from the atmosphere, the...
The Phosphorus Cycle01:21

The Phosphorus Cycle

Unlike carbon, water, and nitrogen, phosphorus is not present in the atmosphere as a gas. Instead, most phosphorus in the ecosystem exists as compounds, such as phosphate ions (PO43-), found in soil, water, sediment and rocks. Phosphorus is often a limiting nutrient (i.e., in short supply). Consequently, phosphorus is added to most agricultural fertilizers, which can cause environmental problems related to runoff in aquatic ecosystems.

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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
05:47

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

Published on: June 25, 2020

Plant phosphoproteomics: an update.

Birgit Kersten1, Ganesh Kumar Agrawal, Pawel Durek

  • 1Max Planck Institute for Molecular Plant Physiology, Potsdam-Golm, Germany. kersten@mpimp-golm.mpg.de

Proteomics
|February 13, 2009
PubMed
Summary
This summary is machine-generated.

This review updates plant phosphoproteomics, detailing advances in identifying and quantifying phosphorylation sites. New computational tools improve prediction accuracy, aiding understanding of plant cellular processes.

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Area of Science:

  • Plant biology
  • Molecular biology
  • Biochemistry

Background:

  • Phosphoproteomics identifies phosphoproteins and phosphorylation sites to understand biological functions.
  • Systematic phosphoproteomic analyses in plants are advancing in vitro and in vivo technologies.
  • Discovering novel protein kinase substrates is crucial for understanding plant signaling.

Purpose of the Study:

  • To provide an update on phosphoproteomic studies in plants.
  • To summarize recent progress in computational prediction of plant phosphorylation sites.
  • To discuss the application of experimental and computational results in plant phosphoproteomic networks.

Main Methods:

  • Systematic phosphoproteomic analyses using optimized in vitro and in vivo technologies.
  • Development of tools like kinase assays with plant protein microarrays for substrate identification.
  • Creation of plant-specific web resources and computational prediction methods for phosphorylation sites.

Main Results:

  • Progress in quantitative and dynamic analysis of mapped phosphorylation sites.
  • Development of computational prediction methods with improved sensitivity and specificity for plant phosphorylation sites.
  • Increased availability of experimentally verified phosphorylation sites in plants.

Conclusions:

  • Recent advancements enhance the identification and quantification of plant phosphorylation sites.
  • Computational prediction tools are significantly improving the detection of phosphorylation sites in plants.
  • Understanding plant phosphoproteomic networks is advanced by integrating experimental and computational findings.