Related Experiment Video
Updated: May 27, 2025

Using TgVtg1:mcherry Zebrafish Embryos to Test the Estrogenic Effects of Endocrine Disrupting Compounds
Published on: August 8, 2020
A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans
Jimmy H Mo1, Chao Zhai2,3, Kwangsek Jung1
1Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, China.
Abstract:
Vitellogenin is thought to share a common ancestor with human apolipoprotein B (ApoB) for systemic lipid transport. In Caenorhabditis elegans, although a general route for inter-tissue vitellogenin transport has been described, the full mechanism that underlies its intracellular trafficking within the intestine remains obscure. In humans, the TANGO1 family of proteins generates membrane carriers to accommodate bulky ApoB-containing lipoprotein particles for their endoplasmic reticulum (ER) export. TANGO1 orthologs have hitherto been discovered in most metazoans, except nematodes. Here, we report the C. elegans TNGL-1 as a mediator of vitellogenin export from the ER. Depletion of TNGL-1 causes the retention of vitellogenin in the ER lumen. Furthermore, the TNGL-1 C-terminal unstructured domain and its luminal globular domain are required for its proper localization and cargo engagement, respectively. Our findings support TNGL-1 as a distant TANGO1 family member and point to the universal requirement of TANGO1-based mechanisms for the secretion of specific metazoan proteins.
Related Concept Videos
Tail-anchoring of Proteins in the ER Membrane
Directing Proteins to the Rough Endoplasmic Reticulum
Vesicular Tubular Clusters
With the help of motor proteins such...
Protein Transport to the Thylakoids
Protein Transport to the Inner Chloroplast Membrane
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

