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Related Concept Videos

Transport Across the Golgi01:26

Transport Across the Golgi

While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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...
Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...

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Related Experiment Video

Updated: Jul 13, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

Rab22B's role in trans-Golgi network membrane dynamics.

Ee Ling Ng1, Ya Wang, Bor Luen Tang

  • 1Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive, Singapore 117597, Singapore.

Biochemical and Biophysical Research Communications
|August 7, 2007
PubMed
Summary

The small GTPase Rab22B is brain-enriched and localizes to the trans-Golgi network (TGN). Its overexpression disrupts TGN46 localization, suggesting Rab22B

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • The small GTPase Rab22B (also known as Rab31) is implicated in trans-Golgi network (TGN) trafficking.
  • Its precise cellular localization, tissue distribution, and functional roles remain largely uncharacterized.

Purpose of the Study:

  • To investigate the cellular localization, tissue expression, and function of Rab22B.
  • To elucidate Rab22B's role in protein trafficking pathways.

Main Methods:

  • Generation of a specific antibody against Rab22B.
  • Immunofluorescence microscopy to determine cellular localization in HeLa cells.
  • Overexpression studies using wild-type Rab22B and a GDP-binding mutant (Rab22BSN).
  • Analysis of TGN resident proteins and transport assays.

Main Results:

  • Rab22B is enriched in the brain, with significant levels in the spleen and intestine.
  • Endogenous Rab22B primarily localizes to the TGN in HeLa cells.
  • Overexpression of Rab22BSN specifically disrupts the TGN localization of TGN46, a TGN-plasma membrane cycling marker.
  • Rab22BSN overexpression inhibits cell surface transport of VSV-G protein, indicating a role in anterograde TGN exit.
  • Other TGN and endosomal markers, as well as Shiga toxin B subunit transport, were unaffected.

Conclusions:

  • Rab22B is a brain-enriched protein localized to the TGN.
  • Rab22B plays a role in anterograde protein transport from the TGN.
  • A specific C-terminal domain of Rab22B is crucial for its function in TGN trafficking.