cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites.
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.
Mesh Terms:
Antigens, Neoplasm, Aryl Hydrocarbon Receptor Nuclear Translocator, COP-Coated Vesicles, Carrier Proteins, Cell Line, Transformed, Collagen, Endoplasmic Reticulum, HeLa Cells, Humans, Membrane Proteins, Neoplasm Proteins, Protein Binding, Protein Transport, Receptors, Cell Surface
Antigens, Neoplasm, Aryl Hydrocarbon Receptor Nuclear Translocator, COP-Coated Vesicles, Carrier Proteins, Cell Line, Transformed, Collagen, Endoplasmic Reticulum, HeLa Cells, Humans, Membrane Proteins, Neoplasm Proteins, Protein Binding, Protein Transport, Receptors, Cell Surface
Mol. Biol. Cell
Date: Jul. 01, 2011
PubMed ID: 21525241
View in: Pubmed Google Scholar
Download Curated Data For This Publication
209048
Switch View:
- Interactions 5