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Emerging mechanisms of mRNP remodeling regulation

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The assembly and remodeling of the components of messenger ribonucleoprotein particles (mRNPs) are important in determining the fate of a messenger RNA (mRNA). A combination of biochemical and cell biology research, recently complemented by genome‐wide high‐throughput approaches, has led to significant progress on understanding the formation, dynamics, and function of mRNPs. These studies also advanced the challenging process of identifying the evolving constituents of individual mRNPs at various stages during an mRNA's lifetime. While research on mRNP remodeling in general has been gaining momentum, there has been relatively little attention paid to the regulatory aspect of mRNP remodeling. Here, we discuss the results of some new studies and potential mechanisms for regulation of mRNP remodeling. WIREs RNA 2014, 5:713–722. doi: 10.1002/wrna.1241 This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications
A model illustrating how reversible phosphorylation (designated by P) in the intrinsically disordered regions (IDRs; represented by curvy orange lines) near the PAM2 motif may regulate interaction between the C‐terminal MLLE domain of eukaryotic PABPC1 and a PAM2‐containing protein. RRM, RNA recognition motif. Details are described in the text.
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A schematic diagram showing key messenger ribonucleoprotein particle (mRNP) remodeling steps during export of a mature mRNP from the nucleus to the cytoplasm. NPC, nuclear pore complex. Details are described in the text.
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A hypothetical scheme for remodeling of HuR‐associated messenger ribonucleoprotein particles (mRNPs) by p97 segregase activity through nondegradative ubiquitin signaling. Note that HuR has three RNA recognition motifs (RRMs). The first two RRMs bind HuR to the ARE in the initial mRNP. Subsequent ubiquitination of RRM3 leads to recruitment of UBXD8 and p97. ATP hydrolysis by p97 changes its conformation and ‘extracts’ HuR from the mRNA and its mRNP. Details are described in the text.
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