The Clothes Make the mRNA: Past and Present Trends in mRNP Fashion.
Guramrit Singh, Gabriel Pratt, Gene W Yeo, Melissa J Moore
Annual review of biochemistry · 2015 · Vol. 84 · pp. 325-54
Abstract
Throughout their lifetimes, messenger RNAs (mRNAs) associate with proteins to form ribonucleoproteins (mRNPs). Since the discovery of the first mRNP component more than 40 years ago, what is known as the mRNA interactome now comprises >1,000 proteins. These proteins bind mRNAs in myriad ways with varying affinities and stoichiometries, with many assembling onto nascent RNAs in a highly ordered process during transcription and precursor mRNA (pre-mRNA) processing. The nonrandom distribution of major mRNP proteins observed in transcriptome-wide studies leads us to propose that mRNPs are organized into three major domains loosely corresponding to 5' untranslated regions (UTRs), open reading frames, and 3' UTRs. Moving from the nucleus to the cytoplasm, mRNPs undergo extensive remodeling as they are first acted upon by the nuclear pore complex and then by the ribosome. When not being actively translated, cytoplasmic mRNPs can assemble into large multi-mRNP assemblies or be permanently disassembled and degraded. In this review, we aim to give the reader a thorough understanding of past and current eukaryotic mRNP research.
Funding 9 grants
| Grant | Funder |
|---|---|
| R01 HG004659 | NHGRI NIH HHS (United States) |
| Howard Hughes Medical Institute (United States) | |
| U54 HG007005 | NHGRI NIH HHS (United States) |
| U54HG007005 | NHGRI NIH HHS (United States) |
| R01 NS075449 | NINDS NIH HHS (United States) |
| HG004659 | NHGRI NIH HHS (United States) |
| NS075449 | NINDS NIH HHS (United States) |
| R01 GM053007 | NIGMS NIH HHS (United States) |
| GM53007 | NIGMS NIH HHS (United States) |