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Related Concept Videos

Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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

Export of Misfolded Proteins out of the ER

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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...
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Updated: Sep 17, 2025

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

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ESCRTing the RABs through conversion.

Jachen A Solinger1, Daniel P Ott1, Anne Spang1

  • 1Biozentrum, University of Basel, Basel, Switzerland.

Biochemical Society Transactions
|July 3, 2025
PubMed
Summary
This summary is machine-generated.

The endosomal sorting complex required for transport (ESCRT) machinery regulates cargo degradation and Rab conversion, crucial for endosome maturation. This review clarifies the connection between ESCRT functions and Rab conversion in cellular pathways.

Keywords:
ESCRTRABEX5Rab GTPasesRab conversionendosome maturation

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cellular Communication

Background:

  • The endosomal system is vital for intracellular and intercellular communication.
  • Early endosomes sort ubiquitinated cargo for degradation via ESCRT complexes.
  • Endosome maturation involves Rab conversion and intraluminal vesicle formation.

Purpose of the Study:

  • To review the role of ESCRT machinery in cargo degradation.
  • To examine RABEX5 regulation and MON1/CCZ1-mediated Rab conversion.
  • To propose a model for ESCRT's regulatory role in endosome maturation.

Main Methods:

  • Literature review of recent studies on ESCRT and endosome maturation.
  • Analysis of the relationship between ESCRT functions and Rab conversion.
  • Integration of knowledge on ESCRT machinery, RABEX5, and Rab conversion.

Main Results:

  • ESCRT machinery is essential for packaging ubiquitinated cargo into intraluminal vesicles for degradation.
  • Rab conversion (Rab5 to Rab7) is mediated by the RABEX5-MON1/CCZ1 cascade.
  • Recent studies highlight the interconnectedness of ESCRT functions and Rab conversion.

Conclusions:

  • ESCRT machinery plays a key regulatory role in endosome maturation.
  • Understanding the interplay between ESCRT and Rab conversion is crucial for comprehending cargo degradation pathways.
  • A proposed model integrates ESCRT functions into the Rab conversion process during endosome maturation.