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Related Experiment Video

Updated: Jul 19, 2026

Immunofluorescent Labeling of Plant Virus and Insect Vector Proteins in Hemipteran Guts

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Published on: May 14, 2021

DBC2 is essential for transporting vesicular stomatitis virus glycoprotein.

Faith K Chang¹, Noriko Sato, Noriko Kobayashi-Simorowski

¹Department of Biological Sciences, Fordham University, 441 E Fordham Road, Bronx, NY 10458, USA.

Journal of Molecular Biology

|October 7, 2006

Summary

The deleted in breast cancer 2 (DBC2) gene is crucial for transporting proteins via microtubules. DBC2 knockdown disrupts this essential cellular process, impacting protein movement from the endoplasmic reticulum to the Golgi apparatus.

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Area of Science:

Molecular Biology
Cell Biology
Cancer Research

Background:

Deleted in breast cancer 2 (DBC2) is a tumor suppressor gene implicated in breast and lung cancers.
DBC2, a member of the RHO GTPase family, possesses a unique C-terminal Broad-Complex/Tramtrack/Bric a Brac (BTB) domain.
Prior research suggests DBC2's involvement in ubiquitination, cell-cycle control, cytoskeleton organization, and protein transport.

Purpose of the Study:

To investigate the specific role of DBC2 in the cellular protein transport pathway.
To elucidate the mechanism by which DBC2 influences protein trafficking within the cell.

Main Methods:

Utilized a vesicular stomatitis virus glycoprotein (VSVG) fused with green fluorescent protein as a model cargo.
Employed knockdown of DBC2 in 293 cells to assess its impact on VSVG transport.
Investigated the dependence of DBC2 mobility on an intact microtubule network.

Main Results:

DBC2 knockdown significantly impaired the vesicular stomatitis virus glycoprotein (VSVG) transport system in 293 cells.
The mobility of DBC2 was found to be dependent on a functional microtubule network.
These findings indicate a direct role for DBC2 in microtubule-mediated protein transport.

Conclusions:

DBC2 plays a critical role in the microtubule-dependent transport of VSVG.
The study establishes DBC2's essential function in facilitating protein movement from the endoplasmic reticulum to the Golgi apparatus.