cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites.

Abstract

Cutaneous T-cell lymphoma-associated antigen 5 (cTAGE5), an originally identified tumor antigen, is overexpressed in various cancer cell lines. The cDNA encodes an integral membrane protein containing two coiled-coil motifs and a proline-rich domain. We show that cTAGE5 specifically localizes to the endoplasmic reticulum (ER) exit sites. In addition, cTAGE5 forms a complex with TANGO1 (MIA3), a previously characterized cargo receptor for collagen VII, by the interaction of their coiled-coil motifs. Of interest, cTAGE5, as well as TANGO1, is capable of interacting with the inner-layer coatomer of COPII Sec23/24 complex through their C-terminal proline-rich domains and required for collagen VII secretion. We propose that cTAGE5 acts as a coreceptor of TANGO1 for collagen VII export from the ER.

• Authors: Kota Saito, Koh Yamashiro, Yuki Ichikawa, Patrik Erlmann, Kenji Kontani, Vivek Malhotra, Toshiaki Katada
• Journal: Molecular biology of the cell (Mol Biol Cell) Vol. 22 Issue 13 Pg. 2301-8 (Jul 01 2011) ISSN: 1939-4586 [Electronic] United States
• PMID: 21525241 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• ARNT protein, human
• Antigens, Neoplasm
• Carrier Proteins
• MIA2 protein, human
• Membrane Proteins
• Neoplasm Proteins
• Receptors, Cell Surface
• serpin-enzyme complex receptor
• Aryl Hydrocarbon Receptor Nuclear Translocator
• Collagen

Topics

• Antigens, Neoplasm (metabolism)
• Aryl Hydrocarbon Receptor Nuclear Translocator (metabolism)
• COP-Coated Vesicles (metabolism)
• Carrier Proteins (metabolism)
• Cell Line, Transformed
• Collagen (metabolism)
• Endoplasmic Reticulum (metabolism)
• HeLa Cells
• Humans
• Membrane Proteins (metabolism)
• Neoplasm Proteins (metabolism)
• Protein Binding
• Protein Transport
• Receptors, Cell Surface (metabolism)