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 Experiment Videos

Rab4 and Rab7 define distinct nonoverlapping endosomal compartments

G Bottger1, B Nagelkerken, P van der Sluijs

  • 1Department of Cell Biology, Utrecht University School of Medicine, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. pvander@knoware.nl

The Journal of Biological Chemistry
|November 15, 1996
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Platelet secretory behaviour: as diverse as the granules … or not?

Journal of thrombosis and haemostasis : JTH·2015
Same author

Optically powered fiber networks.

Optics express·2008
Same author

Rab4 regulates formation of synaptic-like microvesicles from early endosomes in PC12 cells.

Molecular biology of the cell·2001
Same author

Glycosphingolipids are required for sorting melanosomal proteins in the Golgi complex.

The Journal of cell biology·2001
Same author

PDGF-regulated rab4-dependent recycling of alphavbeta3 integrin from early endosomes is necessary for cell adhesion and spreading.

Current biology : CB·2001
Same author

How proteins move lipids and lipids move proteins.

Nature reviews. Molecular cell biology·2001
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

Rab4 and Rab7 GTPases regulate distinct endocytic pathway compartments. Studies show Rab4 is in early endosomes, while Rab7 is in late endosomes, indicating separate cellular roles.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Endocytosis Research

Background:

  • Rab GTPases are key regulators of intracellular membrane trafficking.
  • Rab4 and Rab7 are known to localize to different endosomal compartments.
  • Their precise functional and spatial relationship within the endocytic pathway remains unclear.

Purpose of the Study:

  • To investigate whether Rab4 and Rab7 function in related or distinct intracellular compartments.
  • To characterize novel antibodies for Rab4 detection and immunoisolation.
  • To determine the spatial distribution of Rab4 and Rab7 within the endocytic pathway.

Main Methods:

  • Generation of stable cell lines expressing a novel hemagglutinin (NH)-tagged Rab4.
  • Characterization of anti-NH antibodies for immunoisolation.

Related Experiment Videos

  • Immunoisolation of endocytic vesicles containing NH-Rab4.
  • Analysis of immunoisolated vesicles for Rab7 and internalized transferrin.
  • Confocal immunofluorescence microscopy to assess codistribution of Rab4, Rab5, and Rab7.

    • Main Results:

    • NH-Rab4 expressing cells allowed immunoisolation of endocytic vesicles.
    • Immunoisolated vesicles contained internalized transferrin but lacked Rab7.
    • Confocal microscopy revealed no codistribution of Rab4 and Rab7, nor Rab5 and Rab7, within the same cell.
    • Rab4 and Rab5, known early endosomal markers, were spatially separated from Rab7.

    Conclusions:

    • Rab4 and Rab7 reside in distinct intracellular compartments within the endocytic pathway.
    • Each Rab GTPase (Rab4, Rab5, Rab7) appears to define a specific functional station.
    • This supports a model of spatially segregated Rab GTPase functions in endocytosis.