TY - JOUR TI - A stress assembly that confers cell viability by preserving ERES components during amino-acid starvation AU - Zacharogianni, Margarita AU - Aguilera-Gomez, Angelica AU - Veenendaal, Tineke AU - Smout, Jan AU - Rabouille, Catherine A2 - Nunnari, Jodi VL - 3 PY - 2014 DA - 2014/11/11 SP - e04132 C1 - eLife 2014;3:e04132 DO - 10.7554/eLife.04132 UR - https://doi.org/10.7554/eLife.04132 AB - Nutritional restriction leads to protein translation attenuation that results in the storage and degradation of free mRNAs in cytoplasmic assemblies. In this study, we show in Drosophila S2 cells that amino-acid starvation also leads to the inhibition of another major anabolic pathway, the protein transport through the secretory pathway, and to the formation of a novel reversible non-membrane bound stress assembly, the Sec body that incorporates components of the ER exit sites. Sec body formation does not depend on membrane traffic in the early secretory pathway, yet requires both Sec23 and Sec24AB. Sec bodies have liquid droplet-like properties, and they act as a protective reservoir for ERES components to rebuild a functional secretory pathway after re-addition of amino-acids acting as a part of a survival mechanism. Taken together, we propose that the formation of these structures is a novel stress response mechanism to provide cell viability during and after nutrient stress. KW - protein transport through the secretory pathway KW - amino-acid starvation KW - ER exit site KW - COPII KW - liquid droplet KW - stress granule JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -