Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Simulated Microgravity Enhances Germ Tube Elongation by <i>Golovinomyces cichoracearum</i> on <i>Cucurbita pepo</i> and <i>Arabidopsis thaliana</i> Leaves.

Phytopathology·2025
Same author

GLARE: discovering hidden patterns in spaceflight transcriptome using representation learning.

NPJ microgravity·2025
Same author

Application of Open-Source Digital Resources for 3D Visualization of Clustered Transcriptomic Data.

Physiologia plantarum·2025
Same author

Chromatin structures from integrated AI and polymer physics model.

PLoS computational biology·2025
Same author

Light has a principal role in the Arabidopsis transcriptomic response to the spaceflight environment.

NPJ microgravity·2024
Same author

Single-molecule long-read methylation profiling reveals regional DNA methylation regulated by Elongator Complex Subunit 2 in Arabidopsis roots experiencing spaceflight.

Biology direct·2024

Related Experiment Video

Updated: May 19, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

14-3-3 phosphoprotein interaction networks - does isoform diversity present functional interaction specification?

Anna-Lisa Paul1, Fiona C Denison, Eric R Schultz

  • 1Program in Plant Molecular and Cellular Biology, Horticultural Science Department, University of Florida Gainesville, FL, USA.

Frontiers in Plant Science
|August 31, 2012
PubMed
Summary

Arabidopsis 14-3-3 proteins are key signaling nodes. This study provides evidence that sequence diversity among these proteins indicates functional specificity, impacting signal transduction research.

Keywords:
14-3-3 isoform specificityArabidopsisGRFplantsubcellular localization

More Related Videos

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Related Experiment Videos

Last Updated: May 19, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Area of Science:

  • Plant molecular biology
  • Proteomics
  • Signal transduction

Background:

  • 14-3-3 proteins are crucial phosphoprotein interactors in plants.
  • They form a central hub in the Arabidopsis Interactome Map, mediating numerous signaling pathways.
  • Evidence suggests potential isoform-specific functions, but also functional redundancy among 14-3-3 family members.

Purpose of the Study:

  • To investigate whether sequence diversity in Arabidopsis 14-3-3 protein isoforms correlates with functional diversity at biochemical or cellular levels.
  • To resolve the debate on functional specificity versus redundancy of 14-3-3 isoforms.

Main Methods:

  • Review and discussion of existing observations on 14-3-3 protein function.
  • Presentation of contrastable observations to support the hypothesis of functional diversity.
  • Development of a model to explain 14-3-3 isoform specificity.

Main Results:

  • The study presents a model strongly suggesting functional specificities among Arabidopsis 14-3-3 isoforms.
  • Sequence diversity is indicative of distinct biochemical or cellular roles.

Conclusions:

  • Functional specificities exist within the Arabidopsis 14-3-3 protein family.
  • 14-3-3 diversity and specificity should be considered in signal transduction research and experimental design.