Post-transcriptional processes critically affect eukaryotic gene expression. Cells respond to environmental and
intrinsic stresses by arresting global translation and inducing the accumulation of mRNAs into cytoplasmic RNA granules
such as stress granules (SGs) and processing bodies (PBs), which are thought to participate in the regulation of translation
and degradation of mRNAs. Stresses trigger the formation of SGs and increase PB size and abundance, and the two granules
can share specific mRNAs and proteins. The protein content and dynamics of RNA granules have been extensively
studied, but the mechanisms of interaction of RNA-binding proteins (RBPs) with binding partners and the signaling pathways
that regulate these interactions are poorly understood. Post-translational modification of proteins in RNA granules
via phosphorylation, glycosylation and methylation, influences their associations, enzymatic activities and intracellular locations.
There is evidence that the post-translational modification of RBPs has a major influence on their binding to
mRNA as well as on the assembly of RNA granules. In this review, recent findings concerning the post-translational
modification of RBPs and their possible roles in the assembly of RNA granules are discussed.
Keywords: Processing bodies, post-transcriptional regulation, post-translational modification, RNA binding proteins, stress granules, translation, granules, stress, CR, ARE, CYTOPLASMIC RNA GRANULES.
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