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Review
. 2010 Nov-Dec;1(3):486-93.
doi: 10.1002/wrna.23.

The role of posttranslational modifications in the assembly of stress granules

Takbum Ohn  1 , Paul Anderson
Affiliations
Review

The role of posttranslational modifications in the assembly of stress granules

Takbum Ohn et al. Wiley Interdiscip Rev RNA. 2010 Nov-Dec.

Abstract

Stress granules (SGs) are aggregates of translationally silenced messenger ribonucleoprotein (mRNP) complexes induced by oxidative, osmotic, hypoxic, thermal, viral, and genotoxic stresses. Over the past decade, extensive research has identified key components of SGs, their molecular interactions, and impact on stress-induced reprogramming of protein expression and cell survival. However, studies defining the signaling pathways that modulate SG assembly have only been launched recently. These studies reveal that posttranslational modifications of selected SG proteins play important roles in the regulation of SG assembly and function. Here we provide an overview of the signaling pathways and posttranslational protein modifications that regulate the assembly and function of SGs.

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Figures

Figure 1
Figure 1
Hypusination of eIF5A via the polyamine biosynthetic pathway. ODC, ornithine decarboxylase; DHS, deoxyhypusine synthase; DOHH, deoxyhypusine hydroxylase. N1‐Guanyl‐1,7‐diaminoheptane (GC7) is a competitive inhibitor of DHS.
Figure 2
Figure 2
Depletion of eukaryotic translation elongation factor 2 (eEF2) inhibits SG assembly. RDG3 (GFP‐G3BP, SG marker; RFP‐Dcp1a, PB marker) double stable cells were transfected with control (siCONT) or eEF2‐specific (siEEF2) siRNAs, then SGs were induced by treating with sodium arsenite (0.5 mM) for 30 min.
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