The greatest catch: Big game fishing for mRNA-bound proteins

Christopher R Sibley, Jan Attig, Jernej Ule

Research output: Contribution to journalArticlepeer-review


Purification of proteins cross-linked to mRNAs has identified 800 mRNA-binding proteins and their characteristics.From the moment an RNA is transcribed, its fate largely depends on its interactions with RNA-binding proteins (RBPs). RBPs can recognize short sequence motifs (Nova, TDP-43, U2AF65), secondary structures (Staufen-1, DGCR8), post-transcriptional modifications (eIF4E, CBP20), RNA duplexes (AGO1-4, helicases), or bind indiscriminately along transcripts (FUS, helicases). Collectively this dynamic interplay with multiple RBPs in an mRNA's life cycle helps determine the function and metabolism of an mRNA within a cell. Further, genotypic variations in many of these RBPs are responsible for diseases including fragile X syndrome, neurologic disorders and certain forms of cancer [1]. Collectively it makes studying RBP-RNA interactions essential due to the implications in both health and disease.Here we discuss two recent studies from the laboratories of Matthias Hentze [2] and Markus Landthaler [3], which have now globally captured and defined the RBPs bound to mRNAs within cultured human cells. Both identify an unexpected wealth of RBPs, many of which were not previously known to interact with RNA, and greatly expand our understanding of the mRNA interactome.
Original languageEnglish
Article number163
JournalGenome Biology
Issue number7
Publication statusPublished - 17 Jul 2012


  • binding sites
  • humans
  • immunoprecipitation
  • RNA
  • RNA-Binding Proteins
  • messenger


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