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Related Experiment Video

Updated: May 6, 2026

Co-culture of Living Microbiome with Microengineered Human Intestinal Villi in a Gut-on-a-Chip Microfluidic Device

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COPII vesicles get supersized by ubiquitin.

Vivek Malhotra¹

¹Department of Cell and Developmental Biology, Center for Genomic Regulation (CRG) and University of Pompeu Fabra, 08002 Barcelona, Spain. vivek.malhotra@crg.eu

|April 3, 2012

Summary

Large proteins like procollagen fibrils are exported from the endoplasmic reticulum via oversized vesicles. This process is facilitated by the ubiquitination of the COPII component Sec31p.

Area of Science:

Cell Biology
Molecular Biology
Protein Transport

Background:

Conventional COPII-coated vesicles have limitations in transporting large cargo molecules.
Exporting large proteins, such as procollagen fibrils, from the endoplasmic reticulum presents a significant cellular challenge.

Discussion:

The study investigates the mechanism behind the export of oversized cargo from the endoplasmic reticulum.
Focuses on the role of COPII (coat protein complex II) vesicles in large cargo export.

Key Insights:

The ubiquitination of Sec31p, a COPII component, is crucial for the formation of oversized vesicles.
This modification allows for the efficient transport of large proteins that would otherwise be impeded.

Outlook:

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Understanding this mechanism could offer insights into protein secretion disorders.
Further research may explore therapeutic strategies targeting vesicle formation for enhanced protein export.