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

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Molecular Chaperones and Protein Folding03:00

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...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Regulation of Hematopoietic Stem Cells01:01

Regulation of Hematopoietic Stem Cells

All blood and immune cells are produced from the multipotent hematopoietic stem cells (HSCs) by the process of hematopoiesis. However, they all have a limited life span. In addition, many are depleted in immune surveillance or combatting an injury or infection. This makes blood one of the most regenerative tissues. Hematopoiesis helps replenish these blood and immune cells, restoring the body's normal functioning. However, overproduction of blood and immune cells can make them cancerous or...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

You might also read

Related Articles

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

Sort by
Same author

Integrated Single-Cell and Spatial Profiling of MMP Gene Expression in Colorectal Cancer.

bioRxiv : the preprint server for biology·2026
Same author

Interventions to promote resilience in sexual and gender minority youth in the clinical setting: a scoping review.

Journal of pediatric psychology·2026
Same author

The effect of walnut consumption on the peripheral blood mononuclear cell transcriptome.

Genes & nutrition·2026
Same author

Recognizing and Addressing Health Care Barriers for Transgender and Nonbinary People Living With a Chronic Illness or Disability.

Qualitative health research·2025
Same author

Innovation in Medical Education on Intellectual/Developmental Disabilities: Report on the National Inclusive Curriculum for Health Education-Medical Initiative.

Medical care·2024
Same author

Evaluation of UCP1162, a potent propargyl-linked inhibitor of dihydrofolate reductase with potential application to cancer and autoimmune disease.

Biochemical pharmacology·2024

Related Experiment Video

Updated: Jul 7, 2026

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Hsp70B' regulation and function.

Emily J Noonan1, Robert F Place, Charles Giardina

  • 1Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA. emily.noonan@gmail.com

Cell Stress & Chaperones
|January 31, 2008
PubMed
Summary
This summary is machine-generated.

Heat shock protein 70B (Hsp70B) and Hsp70B

More Related Videos

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
07:14

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Published on: March 8, 2024

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

Related Experiment Videos

Last Updated: Jul 7, 2026

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
07:14

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Published on: March 8, 2024

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

Area of Science:

  • Molecular Biology
  • Cellular Stress Response
  • Protein Homeostasis

Background:

  • Heat shock proteins (Hsps) are crucial molecular chaperones involved in cellular stress response.
  • Hsp70B is a strictly inducible human Hsp70 chaperone with minimal basal expression.
  • Understanding the roles of different Hsp70 family members in stress response is vital.

Purpose of the Study:

  • To investigate the coordinated regulation and functional roles of Hsp70B and Hsp72 in human colon cell lines under proteotoxic stress.
  • To determine the specific contributions of Hsp70B and Hsp72 to cellular viability during stress.
  • To explore the differential activation of Hsp70B and Hsp72 by various stressors.

Main Methods:

  • Utilized siRNA to knockdown Hsp70B and Hsp72 expression in HT-29, SW-480, and CRL-1807 colon cell lines.
  • Assayed Hsp70B promoter activity using flow cytometry in HT-29eGFP cells.
  • Exposed cells to heat stress and proteasome inhibitors to induce cellular damage.

Main Results:

  • Hsp70B and Hsp72 are coordinately regulated in response to cellular stress.
  • Proteasome inhibition strongly activates Hsp70B expression.
  • Knockdown of both Hsp70B and Hsp72 increased cell sensitivity to heat and proteasome inhibition.
  • Hsp72 acts as the primary responder to proteotoxic stress, while Hsp70B functions as a secondary responder.
  • ZnSO4 specifically induces Hsp70B in CRL-1807 cells, suggesting stressor-specific roles.
  • Both Hsp70B and Hsp72 are essential for maintaining cell viability under conditions of damaged protein accumulation.

Conclusions:

  • Hsp72 is the primary Hsp70 responder to proteotoxic stress, with Hsp70B acting as a secondary responder.
  • Hsp70B exhibits stressor-specific induction, indicating unique roles in cellular defense.
  • Both Hsp70B and Hsp72 are critical for cell survival during proteotoxic stress.
  • These findings have implications for understanding cell survival in pathological conditions involving protein damage.