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Jose C. Pastor-Pareja¡¯s group reports in Journal of Cell Biology a critical role of TANGO1 in the morphogenesis of ER exit sites

On March 9th 2017, the group of Jose C. Pastor-Pareja in the School of Life Sciences, Tsinghua University, published an article entitled “Tango1 spatially organizes ER exit sites to control ER export” in Journal of Cell Biology. In their work, they characterized the role of the conserved protein TANGO1 in the secretion of collagen and other secretory cargoes by using Drosophila genetics and super-resolution imaging. Based on their findings, they propose a revised model of how cargoes exit the ER. In this model, TANGO1 brings together ER exit site, COPII carrier and Golgi, allowing direct and efficient trafficking of large and small protein cargoes alike.


Exit of secretory cargo from the endoplasmic reticulum (ER) takes place at specialized domains called ER exit sites (ERESs). In mammals, loss of TANGO1 and other MIA/cTAGE (melanoma inhibitory activity/cutaneous T cell lymphoma–associated antigen) family proteins prevents ER exit of large cargoes such as collagen. Here, we show that Drosophila melanogaster Tango1, the only MIA/cTAGE family member in fruit flies, is a critical organizer of the ERES–Golgi interface. Tango1 rings hold COPII (coat protein II) carriers and Golgi in close proximity at their center. Loss of Tango1, present at ERESs in all tissues, reduces ERES size and causes ERES–Golgi uncoupling, which impairs secretion of not only collagen, but also all other cargoes we examined. Further supporting an organizing role of Tango1, its overexpression creates more and larger ERESs. Our results suggest that spatial coordination of ERES, carrier, and Golgi elements through Tango1’s multiple interactions increases secretory capacity in Drosophila and allows secretion of large cargo.

Dr. Min Liu (School of Life Sciences postdoc) and Zhi Feng (School of Life Sciences PhD student) are co-first authors of this paper. Principal Investigator Jose C. Pastor-Pareja is corresponding author. The work was funded by the Natural Science Foundation of China, the Tsinghua University Initiative Scientific Research Program and the 1,000 Talents program.

Figure 1. Tango1 spatially organizes ER exit sites to control cargo export. (Left) Tango1 is found in ring-like structures at ER exit sites, in close proximity or actual direct contact with the cis-Golgi. (Right) Interaction of Tango1 with itself, COPII, Rab1 and Golgi proteins maintains the structural integrity of ERES-Golgi interface and coordinates transfer of cargo from the ER to the Golgi.

Paper links:

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