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

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.5K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.5K
Structural Protein Function01:56

Structural Protein Function

29.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
29.9K
Structural Protein Function01:56

Structural Protein Function

3.3K
3.3K
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.6K
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.6K
Protein and Protein Structure02:15

Protein and Protein Structure

87.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.6K
The Evidence for Evolution02:55

The Evidence for Evolution

48.1K
Genetic variations accumulating within populations over generations give rise to biological evolution. Evolutionary changes can result in the formation of novel varieties and entire new species. These changes are responsible for the diverse forms of life inhabiting the planet. The evidence for evolution suggests that all living organisms descended from common ancestors.
48.1K

You might also read

Related Articles

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

Sort by
Same author

Dosage compensation of Caj1-induced cytotoxicity by Sis1 and Ydj1 reveals complex interactions among JDPs in the yeast cytosol.

Genetics·2026
Same author

The private solution trap in collective action problems across 34 nations.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

PAM18-3, a J-domain protein, maintains mitochondrial integrity and plant growth and development in Arabidopsis thaliana.

The Plant journal : for cell and molecular biology·2026
Same author

Prefoldin 5 is a microtubule-associated protein that suppresses Tau aggregation and neurotoxicity.

eLife·2026
Same author

Origin of class B J-domain proteins involved in amyloid transactions.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

J-domain proteins: from molecular mechanisms to diseases.

Cell stress & chaperones·2025

Related Experiment Video

Updated: Feb 2, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.8K

Function, evolution, and structure of J-domain proteins.

Harm H Kampinga1, Claes Andreasson2, Alessandro Barducci3

  • 1Department of Cell Biology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. h.h.kampinga@umcg.nl.

Cell Stress & Chaperones
|November 28, 2018
PubMed
Summary
This summary is machine-generated.

Heat shock protein 70 (Hsp70) chaperone systems are vital for cellular protein maintenance. This report summarizes expert consensus on J-domain proteins (JDPs), key regulators of Hsp70 function, to guide future research.

Keywords:
8-stranded β-sandwich domain (SBDβ)Heat shock protein 70 (Hsp70)J-domain proteins (JDPs)

More Related Videos

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
09:01

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

31.1K
Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

7.9K

Related Experiment Videos

Last Updated: Feb 2, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.8K
Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
09:01

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

31.1K
Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

7.9K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Hsp70 chaperone systems are essential molecular machines found in all organisms and cellular compartments.
  • They facilitate critical protein processes including folding, trafficking, remodeling, disaggregation, and degradation.
  • Hsp70 function is modulated by co-chaperones, with J-domain containing proteins (JDPs) representing the largest and most functionally significant family.

Framework:

  • A workshop convened experts to discuss the structure, evolution, and function of JDPs.
  • The focus was on understanding the diverse roles JDPs play in specifying and directing Hsp70 activities.
  • Key areas of JDP research and knowledge gaps were identified.

Implementation:

  • The report synthesizes findings and expert consensus from the Gdansk workshop.
  • It aims to provide a cohesive overview of the current understanding of JDPs.
  • Future research directions for the Hsp70 field are outlined.

Implications:

  • Clarifying JDP mechanisms will enhance our understanding of fundamental cellular protein quality control.
  • This knowledge can inform therapeutic strategies targeting protein misfolding diseases.
  • The consensus provides a roadmap for advancing Hsp70 and JDP research globally.