Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Mar 7;7:e32723. doi: 10.7554/eLife.32723

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2018, Raote et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

PMC Copyright notice

Figure 1. — (A) A schematic depiction of full length TANGO1, showing the extent of each domain in amino acids. (B) Three TANGO1-family proteins (TANGO1, TANGO1-short and cTAGE5) that form a stable complex at the ERES (Maeda et al., 2016). TANGO1 is a type one single-pass transmembrane protein of 1907 amino acids, localised to ER exit sites. TANGO1 has an N-terminal lumenal SH3-like domain that interacts with collagen (Saito et al., 2009) via the chaperone, HSP47 (Ishikawa et al., 2016). There is a transmembrane helix and, in close proximity, a membrane insertion helix. On the cytoplasmic side of the ER membrane, TANGO1 has two coiled-coil (CC) domains (CC1 and CC2). CC1 is used by TANGO1 to recruit ERGIC membranes for producing a collagen carrier (Santos et al., 2015). CC2 binds to a similar coiled-coil domain in cTAGE5 (18). The proline-rich domain (PRD) binds ER exit site machinery Sec23 (Saito et al., 2009; Ma and Goldberg, 2016) and Sec16 (Maeda et al., 2017). Alternative splicing of TANGO1 results in a short isoform, TANGO1-short (Wilson et al., 2011), lacking the lumenal domain. The closely related protein cTAGE5 has a similar cytoplasmic domain organisation with two coiled-coil domains (CC1 and CC2) and a proline-rich domain (PRD). Via its CC1 it recruits Sec12 (Saito et al., 2014). cTAGE5 and TANGO1/TANGO1-short interact through their respective CC2 domains. In addition, the cTAGE5 CC2 also interacts with the retrograde v-SNARE Sec22 (Fan et al., 2017). Like the TANGO1/TANGO1-short PRDs, the cTAGE5 PRD also interacts with Sec23 (Ma and Goldberg, 2016; Saito et al., 2011; Wang et al., 2016).

Figure 1—figure supplement 1. — (A) A schematic depiction of full length TANGO1, showing the extent of each domain in amino acids. (B) Three TANGO1-family proteins (TANGO1, TANGO1-short and cTAGE5) that form a stable complex at the ERES (Maeda et al., 2016). TANGO1 is a type one single-pass transmembrane protein of 1907 amino acids, localised to ER exit sites. TANGO1 has an N-terminal lumenal SH3-like domain that interacts with collagen (Saito et al., 2009) via the chaperone, HSP47 (Ishikawa et al., 2016). There is a transmembrane helix and, in close proximity, a membrane insertion helix. On the cytoplasmic side of the ER membrane, TANGO1 has two coiled-coil (CC) domains (CC1 and CC2). CC1 is used by TANGO1 to recruit ERGIC membranes for producing a collagen carrier (Santos et al., 2015). CC2 binds to a similar coiled-coil domain in cTAGE5 (18). The proline-rich domain (PRD) binds ER exit site machinery Sec23 (Saito et al., 2009; Ma and Goldberg, 2016) and Sec16 (Maeda et al., 2017). Alternative splicing of TANGO1 results in a short isoform, TANGO1-short (Wilson et al., 2011), lacking the lumenal domain. The closely related protein cTAGE5 has a similar cytoplasmic domain organisation with two coiled-coil domains (CC1 and CC2) and a proline-rich domain (PRD). Via its CC1 it recruits Sec12 (Saito et al., 2014). cTAGE5 and TANGO1/TANGO1-short interact through their respective CC2 domains. In addition, the cTAGE5 CC2 also interacts with the retrograde v-SNARE Sec22 (Fan et al., 2017). Like the TANGO1/TANGO1-short PRDs, the cTAGE5 PRD also interacts with Sec23 (Ma and Goldberg, 2016; Saito et al., 2011; Wang et al., 2016).