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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
20.7K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
3.4K
Conserved Binding Sites01:49

Conserved Binding Sites

5.3K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.3K
Protein Complex Assembly02:41

Protein Complex Assembly

17.0K
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...
17.0K
Structural Protein Function01:56

Structural Protein Function

3.3K
3.3K
Structural Protein Function01:56

Structural Protein Function

30.4K
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...
30.4K

You might also read

Related Articles

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

Sort by
Same author

Mitochondrial HSP90 Paralog TRAP1 Deletion Drives Glutamine Addiction in Tumor Cells via Destablization of the Cys/Glu Antiporter SLC7A11/xCT.

Molecular cancer research : MCR·2025
Same author

Representation of Social Determinants of Health terminology in medical subject headings: impact of added terms.

Journal of the American Medical Informatics Association : JAMIA·2024
Same author

An update on the status of HSP90 inhibitors in cancer clinical trials.

Cell stress & chaperones·2024
Same author

Analysis of the health economics portfolio funded by the National Institutes of Health in response to published guidance.

PloS one·2024
Same author

Detecting Posttranslational Modifications of Hsp90 Isoforms.

Methods in molecular biology (Clifton, N.J.)·2023
Same author

Structural and functional complexity of HSP90 in cellular homeostasis and disease.

Nature reviews. Molecular cell biology·2023

Related Experiment Video

Updated: Mar 19, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.3K

Clients Place Unique Functional Constraints on Hsp90.

Abbey D Zuehlke1, Len Neckers1

  • 1Urologic Oncologic Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA.

Trends in Biochemical Sciences
|June 15, 2016
PubMed
Summary

Heat shock protein 90 kDa (Hsp90) supports many client proteins, but their specific needs are unclear. This study used yeast to investigate how different clients affect Hsp90 function and yeast health.

Keywords:
Hsp90chaperone-mediated client maturation.molecular chaperone

More Related Videos

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

7.1K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.1K

Related Experiment Videos

Last Updated: Mar 19, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.3K
Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

7.1K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.1K

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Heat shock protein 90 kDa (Hsp90) is a crucial molecular chaperone.
  • Hsp90 facilitates the conformational maturation and stability of a wide array of client proteins.
  • The specific functional requirements of individual Hsp90 clients are not well understood.

Purpose of the Study:

  • To investigate the constraints imposed on Hsp90 by distinct client proteins.
  • To explore the relationship between these client-imposed constraints and overall yeast fitness.

Main Methods:

  • Utilized yeast growth assays.
  • Employed mutational analysis to probe Hsp90-client interactions.

Main Results:

  • Identified varying functional requirements for different Hsp90 clients.
  • Demonstrated a link between client-specific Hsp90 constraints and yeast fitness.

Conclusions:

  • The functional demands of Hsp90 clients are diverse.
  • Understanding client-specific constraints on Hsp90 is important for predicting cellular fitness.