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Related Concept Videos

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...
Rab Cascades01:25

Rab Cascades

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.
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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...
Rab Proteins01:14

Rab Proteins

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...
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...
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...

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Related Experiment Video

Updated: May 27, 2026

Examination of the Telomere G-overhang Structure in Trypanosoma brucei
15:25

Examination of the Telomere G-overhang Structure in Trypanosoma brucei

Published on: January 26, 2011

Rab28 function in trypanosomes: interactions with retromer and ESCRT pathways.

Jennifer H Lumb1, Ka Fai Leung, Kelly N Dubois

  • 1Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.

Journal of Cell Science
|November 22, 2011
PubMed
Summary
This summary is machine-generated.

Rab28 is crucial for protein turnover and lysosomal delivery in Trypanosoma brucei. This GTPase regulates both retromer-dependent recycling and ESCRT-mediated degradation pathways.

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Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers (Diethylaminoethyl-cellulose Columns)
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Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers (Diethylaminoethyl-cellulose Columns)

Published on: April 6, 2019

RNA Catalyst as a Reporter for Screening Drugs against RNA Editing in Trypanosomes
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RNA Catalyst as a Reporter for Screening Drugs against RNA Editing in Trypanosomes

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Related Experiment Videos

Last Updated: May 27, 2026

Examination of the Telomere G-overhang Structure in Trypanosoma brucei
15:25

Examination of the Telomere G-overhang Structure in Trypanosoma brucei

Published on: January 26, 2011

Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers (Diethylaminoethyl-cellulose Columns)
14:26

Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers (Diethylaminoethyl-cellulose Columns)

Published on: April 6, 2019

RNA Catalyst as a Reporter for Screening Drugs against RNA Editing in Trypanosomes
09:19

RNA Catalyst as a Reporter for Screening Drugs against RNA Editing in Trypanosomes

Published on: July 22, 2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Parasitology

Background:

  • Early endosomal cargo follows either degradation or recycling pathways.
  • Retromer and ESCRT complexes manage late endosome/multivesicular body functions.
  • Mechanisms coordinating these pathways are largely unknown, but Rab GTPases are key regulators.

Purpose of the Study:

  • Investigate the role of Rab28 in endosomal trafficking in Trypanosoma brucei.
  • Determine if Rab28 interacts with or regulates retromer and ESCRT complexes.
  • Elucidate the coordination of degradative and recycling pathways.

Main Methods:

  • Localization studies of Rab28 within the endosomal pathway.
  • RNA interference (RNAi) to deplete Rab28.
  • Analysis of protein levels for ESCRT I and retromer components.
  • Assessment of endocytosed protein turnover and lysosomal delivery.

Main Results:

  • Rab28 localizes to the endosomal pathway and partially overlaps with Vps23 (ESCRT I component).
  • Rab28 depletion impairs endocytosed protein turnover and lysosomal delivery.
  • Rab28 deficiency leads to reduced protein levels of ESCRT I (Vps23/28) and retromer (Vps26).

Conclusions:

  • Rab28 is essential for efficient protein degradation and lysosomal targeting in Trypanosoma brucei.
  • Rab28 acts as a key regulator of both ESCRT-dependent degradation and retromer-dependent trafficking.
  • Rab28 coordinates the interplay between these critical endosomal pathways.