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Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates
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Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates
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Journal Article
Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates
2003
Overview
60S and 40S ribosomal subunits are assembled in the nucleolus and exported from the nucleus to the cytoplasm independently of each other. We show that in vertebrate cells, transport of both subunits requires the export receptor CRM1 and Ran·GTP. Export of 60S subunits is coupled with that of the nucleo‐ cytoplasmic shuttling protein NMD3. Human NMD3 (hNMD3) contains a CRM‐1‐dependent leucine‐rich nuclear export signal (NES) and a complex, dispersed nuclear localization signal (NLS), the basic region of which is also required for nucleolar accumulation. When present in
Xenopus
oocytes, both wild‐type and export‐defective mutant hNMD3 proteins bind to newly made nuclear 60S pre‐export particles at a late step of subunit maturation. The export‐defective hNMD3, but not the wild‐type protein, inhibits export of 60S subunits from oocyte nuclei. These results indicate that the NES mutant protein competes with endogenous wild‐type frog NMD3 for binding to nascent 60S subunits, thereby preventing their export. We propose that NMD3 acts as an adaptor for CRM1–Ran·GTP‐mediated 60S subunit export, by a mechanism that is conserved from vertebrates to yeast.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Oxford University Press
Subject
/ Active Transport, Cell Nucleus
/ Animals
/ EMBO20
/ EMBO31
/ Female
/ Humans
/ Mutation
/ NMD3
/ Nuclear Localization Signals - genetics
/ ran GTP-Binding Protein - metabolism
/ Receptors, Cytoplasmic and Nuclear
/ Recombinant Fusion Proteins - chemistry
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ ribosome
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - genetics
/ RNA-Binding Proteins - metabolism
/ Sequence Homology, Amino Acid
/ Yeasts
