Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

Protein Complex Assembly

Protein Complex Assembly

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...

Assembly of Signaling Complexes

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,...

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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...

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

You might also read

Related Articles

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

Sort by

Same author

Hsp90: A means to an end.

Cell stress & chaperones·2026

Same author

Nuclear Type I Myosins are Essential for Life and Genome Organization.

bioRxiv : the preprint server for biology·2024

Same author

TRiC/CCT Chaperonin Governs RNA Polymerase II Activity in the Nucleus to Support RNA Homeostasis.

bioRxiv : the preprint server for biology·2024

Same author

Establishing Order Through Disorder by the Hsp90 Molecular Chaperone.

Journal of molecular biology·2024

Same author

Protocol for establishing a protein interactome based on close physical proximity to a target protein within live budding yeast.

STAR protocols·2023

Same author

The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions.

Molecular cell·2023

Search research articles

Related Experiment Video

Updated: Jul 5, 2026

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

HSP90: the Rosetta stone for cellular protein dynamics?

Diane C Dezwaan¹, Brian C Freeman

¹Department of Cell and Developmental Biology, University of Illinois, Urbana, Illinois, USA.

Cell Cycle (Georgetown, Tex.)

|April 17, 2008

Summary

The heat shock protein 90 (Hsp90) chaperone network drives dynamic protein behaviors essential for cellular homeostasis. Its inherent properties position Hsp90 to regulate cellular environments and protein assembly.

More Related Videos

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Related Experiment Videos

Last Updated: Jul 5, 2026

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Area of Science:

Molecular biology
Cellular dynamics
Protein biochemistry

Background:

The heat shock protein 90 (Hsp90) proteomic network is extensive, involving numerous cellular processes.
The precise functional significance of Hsp90's broad interactions remains largely undefined.
Hsp90 operates within both the cytoplasm and nucleoplasm.

Purpose of the Study:

To elucidate the role of the Hsp90 molecular chaperone machinery in promoting dynamic client protein behaviors.
To explain how Hsp90 contributes to maintaining cellular homeostasis.
To highlight the unique position of molecular chaperones in driving cellular dynamics.

Main Methods:

Proteomic network analysis
Functional significance assessment
Exploration of inherent chaperone properties

Main Results:

Hsp90 machinery promotes dynamic client protein behaviors crucial for homeostasis.
Rapid action of cellular factors, facilitated by Hsp90, enables proper complex assembly.
Efficient transitions between distinct protein structures are supported by Hsp90.

Conclusions:

Molecular chaperones, particularly Hsp90, are uniquely positioned to drive dynamic cellular environments.
Hsp90's inherent properties are critical for regulating protein behavior and cellular function.
Understanding Hsp90's network is key to comprehending cellular homeostasis and dynamics.