Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
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...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Real-world use of PSMA imaging in metastatic castration-sensitive prostate cancer: Findings from the CAPRI-3 registry.

European journal of nuclear medicine and molecular imaging·2026
Same author

Pre-transfusion Testing in Cervical Spine Surgery: Are We Overprepared?

Revista espanola de cirugia ortopedica y traumatologia·2026
Same author

Transceiver 16-Channel Coaxial-End Dipole Array for Combined Head and C-Spine MRI at 9.4 T.

NMR in biomedicine·2026
Same author

An array of paired folded-end dipoles for whole-brain imaging at 9.4 T.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2024
Same author

Evaluation of coaxial dipole antennas as transceiver elements of human head array for ultra-high field MRI at 9.4T.

Magnetic resonance in medicine·2023
Same author

Maize resistance to witchweed through changes in strigolactone biosynthesis.

Science (New York, N.Y.)·2023

Related Experiment Video

Updated: Jul 4, 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

Predicting sub-Golgi localization of type II membrane proteins.

A D J van Dijk1, D Bosch, C J F ter Braak

  • 1Applied Bioinformatics, PRI, Wageningen UR, Wageningen, The Netherlands.

Bioinformatics (Oxford, England)
|June 20, 2008
PubMed
Summary

Predicting protein localization within the Golgi apparatus is crucial for understanding cellular processes. This study developed a novel predictor for sub-Golgi localization of type II transmembrane proteins, aiding glycomic analysis.

More Related Videos

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

Related Experiment Videos

Last Updated: Jul 4, 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

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

Imaging ATG9A, a Multi-Spanning Membrane Protein
07:20

Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

Area of Science:

  • Cell Biology
  • Biochemistry
  • Bioinformatics

Background:

  • Accurate protein localization is vital for understanding cellular functions, especially within the Golgi apparatus.
  • Subcompartmental Golgi localization impacts glycosylation pathways and SNARE protein sorting, but remains poorly understood.

Purpose of the Study:

  • To develop a computational predictor for sub-Golgi localization of type II transmembrane proteins.
  • To leverage protein structure information for improved localization prediction.

Main Methods:

  • Assembled a dataset of type II transmembrane proteins with experimentally verified sub-Golgi localizations.
  • Developed a Support Vector Machine (SVM) predictor utilizing a protein structure-based kernel focused on the transmembrane domain.

Main Results:

  • Successfully developed a predictor for sub-Golgi protein localization.
  • Demonstrated the predictor's applicability on a glycomic scale, revealing significant correlations between localization and glycan biosynthesis.
  • Highlighted the importance of the transmembrane domain in determining sub-Golgi localization.

Conclusions:

  • The developed predictor offers a powerful tool for analyzing protein localization within the Golgi apparatus.
  • This approach enhances our understanding of the relationship between protein localization and glycan biosynthesis.
  • The findings have implications for both fundamental cell biology and applied glycomics.