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Related Concept Videos

ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
The Unfolded Protein Response01:37

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...
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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

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Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange
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Structure-function Studies in Mouse Embryonic Stem Cells Using Recombinase-mediated Cassette Exchange

Published on: April 27, 2017

The ESCRT pathway.

William M Henne1, Nicholas J Buchkovich, Scott D Emr

  • 1Weill Institute for Cell and Molecular Biology, Cornell University, Weill Hall, Ithaca, NY 14853, USA.

Developmental Cell
|July 19, 2011
PubMed
Summary
This summary is machine-generated.

The endosomal sorting complex required for transport (ESCRT) pathway sorts cargo for degradation and shapes membranes. This review examines ESCRT proteins, cargo, and membrane interactions to understand vesicle budding.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Multivesicular bodies (MVBs) are crucial for cellular waste disposal, delivering cargo to the vacuole or lysosome.
  • The endosomal sorting complex required for transport (ESCRT) pathway orchestrates MVB formation and is implicated in viral budding and cell division.
  • Understanding ESCRT's multifaceted roles is key to comprehending fundamental cellular processes.

Purpose of the Study:

  • To provide a comprehensive review of the ESCRT pathway.
  • To analyze ESCRT function from the perspectives of the proteins, their cargo, and membrane dynamics.
  • To elucidate the mechanisms by which ESCRTs drive vesicle budding.

Main Methods:

  • Literature review and synthesis of existing research on the ESCRT pathway.
  • Analysis of ESCRT protein structures and functions.
  • Examination of cargo recognition and sorting mechanisms.
  • Investigation of membrane deformation and scission processes mediated by ESCRTs.

Main Results:

  • The ESCRT pathway functions as a sophisticated cargo-recognition and membrane-sculpting machine.
  • ESCRT proteins interact with specific cargo molecules to mediate their sorting into MVBs.
  • The pathway utilizes a stepwise assembly and disassembly mechanism to deform and bud membranes.

Conclusions:

  • The ESCRT pathway's diverse functions stem from its ability to recognize cargo and sculpt membranes.
  • A deeper understanding of ESCRT-mediated membrane budding is crucial for various cellular processes and diseases.
  • Future research should focus on the dynamic interactions within the ESCRT machinery and its regulation.