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Related Concept Videos

Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Post-translational Translocation of Proteins to the RER01:27

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...
Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
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...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.

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Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
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ESCRT proteins in physiology and disease.

Susanne Stuffers1, Andreas Brech, Harald Stenmark

  • 1Centre for Cancer Biomedicine, Faculty Division, The Norwegian Radium Hospital, University of Oslo, Norway.

Experimental Cell Research
|November 18, 2008
PubMed
Summary

The endosomal sorting complex required for transport (ESCRT) machinery mediates receptor degradation for signal attenuation. ESCRT dysfunction is linked to diseases, and viruses exploit it for budding.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Receptor downregulation via internalization and lysosomal degradation is crucial for signal attenuation.
  • Receptor ubiquitination triggers sorting by the endosomal sorting complex required for transport (ESCRT) machinery.
  • The ESCRT pathway (ESCRT-0, -I, -II, and -III) sorts ubiquitinated proteins and mediates multivesicular endosome biogenesis.

Purpose of the Study:

  • To review the roles of ESCRT proteins in cellular processes.
  • To discuss the involvement of ESCRT dysfunction in various diseases.
  • To highlight the exploitation of the ESCRT pathway by RNA viruses.

Main Methods:

  • Literature review of ESCRT function and associated pathologies.
  • Analysis of ESCRT involvement in receptor trafficking and signal attenuation.
  • Examination of ESCRT roles in viral budding and cytokinesis.

Main Results:

  • ESCRT complexes are essential for degradative endosomal sorting of ubiquitinated membrane proteins.
  • ESCRT dysfunction is implicated in cancer, neurodegenerative diseases, and bacterial infections.
  • Many RNA viruses utilize the ESCRT machinery for their release from host cells.

Conclusions:

  • The ESCRT pathway is vital for regulating cellular signaling and homeostasis.
  • Dysregulation of ESCRT function contributes to significant human diseases.
  • Targeting the ESCRT pathway offers potential therapeutic avenues for viral infections and other pathologies.