Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation

Angelica Aguilera-Gomez; Margarita Zacharogianni; Marinke M van Oorschot; Heide Genau; Rianne Grond; Tineke Veenendaal; Kristina S Sinsimer; Elizabeth R Gavis; Christian Behrends; Catherine Rabouille

doi:10.1016/j.celrep.2017.06.042

Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation

Angelica Aguilera-Gomez, Margarita Zacharogianni, Marinke M van Oorschot, Heide Genau, Rianne Grond, Tineke Veenendaal, Kristina S Sinsimer, Elizabeth R Gavis, Christian Behrends, Catherine Rabouille

Hubrecht Institute

Research output: Contribution to journal/periodical › Article › Scientific › peer-review

17 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	935-948
Number of pages	14
Journal	Cell Reports
Volume	20
Issue number	4
DOIs	https://doi.org/10.1016/j.celrep.2017.06.042
Publication status	Published - 25 Jul 2017

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Journal Article

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10.1016/j.celrep.2017.06.042

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title = "Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation",

abstract = "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.",

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author = "Angelica Aguilera-Gomez and Margarita Zacharogianni and {van Oorschot}, {Marinke M} and Heide Genau and Rianne Grond and Tineke Veenendaal and Sinsimer, {Kristina S} and Gavis, {Elizabeth R} and Christian Behrends and Catherine Rabouille",

year = "2017",

month = jul,

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doi = "10.1016/j.celrep.2017.06.042",

language = "English",

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T1 - Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation

AU - Aguilera-Gomez, Angelica

AU - Zacharogianni, Margarita

AU - van Oorschot, Marinke M

AU - Genau, Heide

AU - Grond, Rianne

AU - Veenendaal, Tineke

AU - Sinsimer, Kristina S

AU - Gavis, Elizabeth R

AU - Behrends, Christian

AU - Rabouille, Catherine

PY - 2017/7/25

Y1 - 2017/7/25

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.

AB - 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.

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DO - 10.1016/j.celrep.2017.06.042

M3 - Article

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SN - 2211-1247

VL - 20

SP - 935

EP - 948

JO - Cell Reports

JF - Cell Reports

IS - 4

ER -

Phospho-Rasputin Stabilization by Sec16 Is Required for Stress Granule Formation upon Amino Acid Starvation

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