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

4.4K
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,...
4.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.3K
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...
14.3K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.3K
4.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
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,...
6.4K
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

8.6K
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
8.6K
Protein Complex Assembly02:41

Protein Complex Assembly

16.4K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.4K

You might also read

Related Articles

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

Sort by
Same author

Molecular perspectives on life-history evolution in Bruchinae seed beetles.

Genetics and molecular biology·2026
Same author

Identification of soybean genotypes resistant to stink bug complex and key agronomic traits for selection.

Brazilian journal of biology = Revista brasleira de biologia·2026
Same author

Natural variation in the ZmPIMT1 promoter enhances seed aging tolerance by regulating PABP2 repair in maize.

The Plant cell·2025
Same author

Bacteriome Signature in SARS-CoV-2-Infected Patients Correlates with Increased Gut Permeability and Systemic Inflammatory Cytokines.

Microorganisms·2025
Same author

Biomolecular condensates-Prerequisites for anhydrobiosis?

Protein science : a publication of the Protein Society·2025
Same author

Genetic variability in soybean with resistance to cyst nematode and powdery mildew: impact of multi-parent crosses on recombination and genetic diversity.

Brazilian journal of biology = Revista brasleira de biologia·2025

Related Experiment Video

Updated: Dec 16, 2025

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

8.8K

Late Embryogenesis Abundant Protein-Client Protein Interactions.

Lynnette M A Dirk1, Caser Ghaafar Abdel2, Imran Ahmad3

  • 1Department of Horticulture, University of Kentucky Seed Biology Program, Plant Science Building, 1405 Veterans Drive, University of Kentucky, Lexington, KY 40546-0312, USA.

Plants (Basel, Switzerland)
|July 3, 2020
PubMed
Summary

Late Embryogenesis Abundant Proteins (LEAPs) protect cellular components from stress by acting as shield molecules or chaperones. Understanding LEAP degradation is key to regulating their cellular abundance and function.

Keywords:
desiccationlate embryogenesis abundantnatural protection and repair mechanismprotein interactionseedstress

More Related Videos

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation
07:16

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation

Published on: January 5, 2024

1.5K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

374

Related Experiment Videos

Last Updated: Dec 16, 2025

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis
05:43

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

8.8K
Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation
07:16

Author Spotlight: Unraveling the Molecular Mechanisms of Brown and Beige Adipocyte Regulation

Published on: January 5, 2024

1.5K
Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

374

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Intrinsically disordered proteins of the Late Embryogenesis Abundant protein (LEAP) family offer protection to intracellular components.
  • LEAPs are crucial for maintaining proteome stability under stress conditions.

Purpose of the Study:

  • To elucidate the protective mechanisms of LEAPs against a stress-susceptible proteome.
  • To investigate the diverse roles of LEAPs in cellular homeostasis and stress mitigation.

Main Methods:

  • Analysis of LEAP interactions with client proteins.
  • Characterization of LEAP functions including shield molecule activity, holdase chaperonin activity, and client protein modulation.
  • Review of documented LEAP-client protein binding instances.

Main Results:

  • LEAPs function as shield molecules, potentially via liquid-liquid phase separation.
  • Some LEAPs act as holdase chaperonins, binding directly to client proteins.
  • LEAPs modulate client protein function, impacting cellular homeostasis and stress mitigation.
  • LEAPs can also facilitate client protein degradation.

Conclusions:

  • LEAP functions are diverse, ranging from direct protection to promoting degradation.
  • Understanding LEAP degradation pathways post-stress is essential for cellular regulation of LEAP abundance.