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

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.7K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

595
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...
595
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.2K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

20.0K
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...
20.0K

You might also read

Related Articles

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

Sort by
Same author

Hypoxia shapes both therapeutic response and resistance in metastatic clear cell renal cell carcinoma.

Cancer cell·2026
Same author

Ninth BHD International Symposium: Advancing research through global collaboration.

Cell stress & chaperones·2026
Same author

Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2.

Cellular and molecular life sciences : CMLS·2026
Same author

Inflammation-Driven Field Cancerization in End-Stage Kidney Disease.

Cancer discovery·2026
Same author

Fanconi anemia complementation group C gene (FANCC) association with hereditary and sporadic renal tumors.

The oncologist·2026
Same author

Targeting and dissociating HIF2α from the molecular chaperone Hsp70 triggers apoptosis in kidney cancer.

Communications medicine·2026

Related Experiment Video

Updated: Feb 18, 2026

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

6.9K

Detecting Posttranslational Modifications of Hsp90.

Rebecca A Sager1,2,3, Mark R Woodford1,2, Len Neckers4

  • 1Department of Urology, SUNY Upstate Medical University, 750 E. Adams Street, Syracuse, NY, 13210, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 28, 2017
PubMed
Summary

Heat Shock Protein 90 (Hsp90) is a crucial molecular chaperone in eukaryotes, vital for protein stability and regulating cancer-driving proteins. Its function relies on ATP binding and hydrolysis, modulated by co-chaperones and posttranslational modifications.

Keywords:
Heat shock protein 90 (Hsp90)Molecular chaperonesPhosphorylationPosttranslational modificationSUMOylationUbiquitination

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

9.2K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Related Experiment Videos

Last Updated: Feb 18, 2026

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

6.9K
Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

9.2K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Heat Shock Protein 90 (Hsp90) is an essential eukaryotic molecular chaperone.
  • Hsp90 plays a critical role in stabilizing proteins involved in multistep carcinogenesis.
  • Its chaperone activity is intrinsically linked to ATP binding and hydrolysis.

Purpose of the Study:

  • To investigate the essential role of Hsp90 in eukaryotic cellular processes.
  • To understand the regulatory mechanisms of Hsp90's ATPase activity.
  • To explore the impact of posttranslational modifications on Hsp90 function.

Main Methods:

  • Expression and purification of Hsp90 from both mammalian and yeast cells.
  • Utilizing immunoblotting techniques to detect Hsp90 posttranslational modifications.
  • Studying the ATP binding and hydrolysis activities of Hsp90.

Main Results:

  • Hsp90's ATPase activity is regulated by co-chaperones and posttranslational modifications like phosphorylation, SUMOylation, and ubiquitination.
  • These modifications are crucial for Hsp90 stability and ATPase regulation.
  • Mammalian and yeast systems provide viable platforms for Hsp90 research.

Conclusions:

  • Hsp90 is a key regulator of protein homeostasis and carcinogenesis.
  • Posttranslational modifications significantly influence Hsp90's stability and function.
  • The study highlights the conserved nature and importance of Hsp90 across different eukaryotic systems.