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

MICAL-1 isoforms, novel rab1 interacting proteins.

Thomas Weide1, Julia Teuber, Michael Bayer

  • 1Department of Experimental Tumorbiology, University of Muenster, Badestr. 9, D-48149, Muenster, Germany.

Biochemical and Biophysical Research Communications
|June 6, 2003
PubMed
Summary

A novel protein, MICAL-1b, interacts with Rab1 GTPases, potentially linking the Golgi apparatus to the cytoskeleton. This discovery expands our understanding of vesicular transport and cellular scaffolding mechanisms.

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

The APOL1 variant p.N264K is predicted to block ion flow by occluding a pore at the cell surface.

Life science alliance·2026
Same author

APOL1 plasma membrane pools resist rapid protein degradation.

Scientific reports·2026
Same author

Mechanisms of Podocyte Injury Due to Loss of the Nucleoporin NUP93.

Journal of the American Society of Nephrology : JASN·2026
Same author

Characterization of LED-based hybrid diffuse reflectance spectroscopy method for determination of SPF and UVA-PF in blinded multi-centre study (ALT-SPF).

International journal of cosmetic science·2025
Same author

Crumbs2 acts as a dynamic cellular sensor triggering stable podocyte cell-matrix anchorage.

Biophysical journal·2025
Same author

A Cell Biologist's View on APOL1: What We Know and What We Still Need to Address.

Cells·2025

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cytoskeletal Dynamics

Background:

  • Rab1 GTPases are crucial for endoplasmic reticulum (ER)-Golgi vesicular transport.
  • Known Rab1 effectors include GM130, p115, and Golgin-84, primarily involved in membrane trafficking.
  • Understanding novel Rab1 interactions is key to deciphering complex cellular transport pathways.

Purpose of the Study:

  • To identify and characterize novel proteins interacting with Rab1 GTPases.
  • To investigate the functional implications of MICAL-1's interaction with Rab1.
  • To explore the potential role of MICAL-1 as a scaffold protein.

Main Methods:

  • Yeast two-hybrid system for identifying protein interactions.
  • GST pulldown assays to confirm interactions.

Related Experiment Videos

  • Cell fractionation to determine protein localization.
  • Mapping of interaction domains.

    • Main Results:

    • MICAL-1b, a MICAL-1a splice variant, specifically interacts with Rab1 in a nucleotide-dependent manner.
    • MICAL-1 exhibits predominantly cytosolic localization, unlike membrane-bound effectors like GM130.
    • The C-terminus of MICAL-1 binds both Rab1 and vimentin, a component of intermediate filaments.

    Conclusions:

    • MICAL-1 isoforms are novel Rab1 interacting proteins.
    • MICAL-1 may act as a scaffold, linking the Golgi apparatus to the intermediate filament cytoskeleton.
    • This interaction provides new insights into the regulation of vesicular transport and cellular organization.