TY  - JOUR
A1  - Aguilera-Gomez, Angelica
A1  - Zacharogianni, Margarita
A1  - Oorschot, Marinke M. van
A1  - Genau, Heide Marika
A1  - Grond, Rianne
A1  - Veenendaal, Tineke
A1  - Sinsimer, Kristina S.
A1  - Gavis, Elizabeth R.
A1  - Behrends, Christian
A1  - Rabouille, Catherine
T1  - Phospho-rasputin stabilization by Sec16 is required for stress granule formation upon amino acid starvation
T2  - Cell Reports
N2  - Most cellular stresses induce protein translation inhibition and stress granule formation. Here, using Drosophila S2 cells, we investigate the role of G3BP/Rasputin in this process. In contrast to arsenite treatment, where dephosphorylated Ser142 Rasputin is recruited to stress granules, we find that, upon amino acid starvation, only the phosphorylated Ser142 form is recruited. Furthermore, we identify Sec16, a component of the endoplasmic reticulum exit site, as a Rasputin interactor and stabilizer. Sec16 depletion results in Rasputin degradation and inhibition of stress granule formation. However, in the absence of Sec16, pharmacological stabilization of Rasputin is not enough to rescue the assembly of stress granules. This is because Sec16 specifically interacts with phosphorylated Ser142 Rasputin, the form required for stress granule formation upon amino acid starvation. Taken together, these results demonstrate that stress granule formation is fine-tuned by specific signaling cues that are unique to each stress. These results also expand the role of Sec16 as a stress response protein.
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/45072
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-450726
SN  - 2211-1247
N1  - This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
VL  - 20
IS  - 4
SP  - 935
EP  - 948
PB  - Cell Press
CY  - Maryland Heights, MO
ER  -