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

Energy to Drive Translocation

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

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...

Export of Misfolded Proteins out of the ER

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...

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

Regulation of the Unfolded Protein Response

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...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

You might also read

Related Articles

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

Sort by

Same author

Current Challenges for the Effective Management of the COVID-19 Pandemic.

Advances in experimental medicine and biology·2022

Same author

Breast Cancer Risk Factors among Ugandan Women at a Tertiary Hospital: A Case-Control Study.

Oncology·2016

Same author

Hyperthermia using nanoparticles--Promises and pitfalls.

International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group·2016

Same author

Positive or negative involvement of heat shock proteins in multiple sclerosis pathogenesis: an overview.

Journal of neuropathology and experimental neurology·2014

Same author

Molecular breast cancer subtypes prevalence in an indigenous Sub Saharan African population.

The Pan African medical journal·2014

Same author

Combined hyperthermia and radiotherapy for the treatment of cancer.

Cancers·2013

Search research articles

Related Experiment Video

Updated: Jul 14, 2026

Intracellular Refolding Assay

Intracellular Refolding Assay

Published on: January 24, 2012

Mechanisms of HSP72 release.

Alexzander Asea¹

¹Division of Investigative Pathology, Scott and White Clinic, Texas A&M University System Health Science Center College of Medicine, 2401 South 31st Street, Temple, TX 76508, USA. asea@medicine.tamhsc.edu

Journal of Biosciences

|May 31, 2007

Summary

Heat shock proteins (HSPs) are released from cells through passive or active mechanisms. This review explores how stress releases HSP72 into circulation and its role in host defense.

Area of Science:

Cellular biology
Immunology

Background:

Two known mechanisms facilitate heat shock protein (HSP) release: passive (necrosis, trauma, surgery, viral infection) and active (non-classical pathway).
HSPs are released as free proteins or within exosomes.

Purpose of the Study:

To review recent findings on the mechanisms of stress-induced heat shock protein 72 (HSP72) release into circulation.
To explore the biological significance of circulating HSP72 in host defense against disease.

Main Methods:

Literature review of recent findings on HSP release mechanisms.
Analysis of stress-induced HSP72 release pathways.
Evaluation of the role of circulating HSP72 in disease.

Main Results:

More Related Videos

Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

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

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 14, 2026

Intracellular Refolding Assay

Intracellular Refolding Assay

Published on: January 24, 2012

Purification of Hsp104, a Protein Disaggregase

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

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

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

Published on: June 7, 2018

Stress can induce HSP72 release into circulation via both passive and active cellular mechanisms.

Circulating HSP72 plays a significant role in the host's defense against various diseases.

Conclusions:

Understanding HSP72 release mechanisms is crucial for comprehending its role in host defense.
Circulating HSP72 represents a key factor in the biological response to cellular stress and disease progression.