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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.

SUBMITTER: Saito K 

PROVIDER: S-EPMC3128532 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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

Saito Kota K   Yamashiro Koh K   Ichikawa Yuki Y   Erlmann Patrik P   Kontani Kenji K   Malhotra Vivek V   Katada Toshiaki T  

Molecular biology of the cell 20110427 13


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 moti  ...[more]

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