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Vol. 15, No. 17, pp. 2215-2228, September 1, 2001
1 Department of Molecular Biology, Yokohama City University
School of Medicine, Yokohama 236-0004, Japan; 2 Biology
Division, National Cancer Center Research Institute, Tokyo 104-0045, Japan
Nonsense-mediated mRNA decay (NMD) is a conserved surveillance
mechanism that eliminates imperfect mRNAs that contain premature translation termination codons (PTCs) and code for nonfunctional or
potentially harmful polypeptides. We show that a novel
phosphatidylinositol 3-kinase-related protein kinase, hSMG-1, is a
human ortholog of a product of Caenorhabditis elegans smg-1,
one of seven smg genes involved in NMD. hSMG-1 phosphorylates
hUPF1/SMG-2 in vivo and in vitro at specific serine residues in SQ
motifs. hSMG-1 can associate with hUPF1/SMG-2 and other components of
the surveillance complex. In particular, overexpression of a
kinase-deficient point mutant of hSMG-1, hSMG-1-DA, results in a marked
suppression of the PTC-dependent 
-globin mRNA degradation; whereas
that of wild-type hSMG-1 enhances it. We also show that inhibitors of
hSMG-1 induce the accumulation of truncated p53 proteins in human
cancer cell lines with p53 PTC mutation. Taken together, we conclude
that hSMG-1 plays a critical role in NMD through the direct
phosphorylation of hUPF1/SMG-2 in the evolutionally conserved mRNA
surveillance complex.
[Key Words: NMD; PIK-related-protein kinase; smg; upf; PTC; p53]
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