Integration of mRNP formation and export

Cell Mol Life Sci. 2017 Aug;74(16):2875-2897. doi: 10.1007/s00018-017-2503-3. Epub 2017 Mar 17.

Abstract

Expression of protein-coding genes in eukaryotes relies on the coordinated action of many sophisticated molecular machineries. Transcription produces precursor mRNAs (pre-mRNAs) and the active gene provides an environment in which the pre-mRNAs are processed, folded, and assembled into RNA-protein (RNP) complexes. The dynamic pre-mRNPs incorporate the growing transcript, proteins, and the processing machineries, as well as the specific protein marks left after processing that are essential for export and the cytoplasmic fate of the mRNPs. After release from the gene, the mRNPs move by diffusion within the interchromatin compartment, making up pools of mRNPs. Here, splicing and polyadenylation can be completed and the mRNPs recruit the major export receptor NXF1. Export competent mRNPs interact with the nuclear pore complex, leading to export, concomitant with compositional and conformational changes of the mRNPs. We summarize the integrated nuclear processes involved in the formation and export of mRNPs.

Keywords: Cell nucleus; Export receptors; Gene expression; Nuclear pore complex; Nucleocytoplasmic export; Polyadenylation; Pre-mRNA processing; Splicing; mRNA; mRNP assembly.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus*
  • Animals
  • Chromatin / genetics
  • Chromatin / metabolism
  • Humans
  • Nuclear Pore / metabolism
  • Polyadenylation
  • Protein Transport
  • RNA Precursors / chemistry
  • RNA Precursors / genetics
  • RNA Precursors / metabolism
  • RNA Splicing
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Ribonucleoproteins / chemistry
  • Ribonucleoproteins / genetics
  • Ribonucleoproteins / metabolism*
  • Transcriptional Activation

Substances

  • Chromatin
  • RNA Precursors
  • RNA, Messenger
  • Ribonucleoproteins
  • messenger ribonucleoprotein