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

The Unfolded Protein Response01:37

The Unfolded Protein Response

5.6K
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...
5.6K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.2K
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...
2.2K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.3K
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...
4.3K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.4K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
4.4K
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

8.3K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
8.3K
The Proteasome01:13

The Proteasome

1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K

You might also read

Related Articles

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

Sort by
Same author

<i>Cryptococcus neoformans</i> rewires the conserved Wee1-CDK checkpoint through two divergent kinases required for replication-stress tolerance and virulence.

bioRxiv : the preprint server for biology·2026
Same author

Integrative Identification of Anti-Photoaging Peptides From Stress-Tolerant Microorganisms via Machine Learning and KEAP1-NRF2 Docking.

Journal of peptide science : an official publication of the European Peptide Society·2026
Same author

Systematic Profiling of Essential Fungal Transcription Factors Uncovers Ezt1 as a Central Pathobiological and Morphogenic Regulator in <i>Cryptococcus neoformans</i>.

Research square·2026
Same author

Performance of FTIR-Based IR Biotyper for Identification and Strain Discrimination of <i>Cryptococcus</i> Species.

Mycobiology·2026
Same author

Deciphering subcellular localization-dependent functions of Hog1 MAPK in Cryptococcus neoformans.

Genetics·2026
Same author

Systematic Profiling of Essential Fungal Transcription Factors Uncovers Ezt1 as a Central Pathobiological and Morphogenic Regulator in <i>Cryptococcus neoformans</i>.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: May 3, 2026

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
10:12

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Published on: June 14, 2024

2.8K

The unfolded protein response (UPR) pathway in Cryptococcus.

Seon Ah Cheon1, Kwang-Woo Jung2, Yong-Sun Bahn2

  • 1Department of Life Science; Research Center for Biomolecules and Biosystems; College of Natural Science; Chung-Ang University; Seoul, Korea; Department of Agricultural Biotechnology and Center for Fungal Pathogenesis; Seoul National University; Seoul, Korea.

Virulence
|February 8, 2014
PubMed
Summary

The unfolded protein response (UPR) pathway in Cryptococcus neoformans is crucial for managing endoplasmic reticulum stress, antifungal resistance, and virulence. This pathway has both conserved and unique features important in cryptococcosis pathogenesis.

Keywords:
Cryptococcus neoformansER stressHxl1Ire1unfolded protein response

More Related Videos

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

1.1K
Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

14.0K

Related Experiment Videos

Last Updated: May 3, 2026

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
10:12

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Published on: June 14, 2024

2.8K
Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

1.1K
Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

14.0K

Area of Science:

  • Microbiology
  • Molecular Biology
  • Mycology

Background:

  • Eukaryotic cells utilize conserved signaling pathways to adapt to environmental cues.
  • The unfolded protein response (UPR) pathway maintains endoplasmic reticulum (ER) homeostasis during cellular stress.
  • Cryptococcus neoformans is an opportunistic fungal pathogen causing meningoencephalitis in immunocompromised individuals.

Purpose of the Study:

  • To review the conserved and unique features of the UPR pathway in Cryptococcus neoformans.
  • To compare the Cryptococcus UPR pathway with those in other fungal species.
  • To elucidate the role of the UPR pathway in the pathogenesis of cryptococcosis.

Main Methods:

  • Comparative analysis of UPR pathway components (Ire1, Hxl1, Kar2/BiP) across fungal species.
  • Review of existing literature on UPR-mediated stress response, drug resistance, and virulence in Cryptococcus neoformans.
  • Examination of Ire1-dependent and -independent functions.

Main Results:

  • The Cryptococcus UPR pathway involves the conserved Ire1 kinase and a unique bZIP transcription factor, Hxl1.
  • The UPR pathway regulates ER stress, antifungal drug resistance, and virulence in an Ire1/Hxl1-dependent manner.
  • Ire1 also plays Hxl1-independent roles in capsule biosynthesis and thermotolerance.

Conclusions:

  • The Cryptococcus UPR pathway exhibits both conserved and unique characteristics compared to other fungi.
  • The UPR pathway is integral to the pathogenesis of cryptococcosis.
  • Further research is needed to fully understand the complexities and therapeutic potential of this pathway.