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. 1988 Oct;8(10):4381–4388. doi: 10.1128/mcb.8.10.4381

The human L-myc gene encodes multiple nuclear phosphoproteins from alternatively processed mRNAs.

J De Greve 1, J Battey 1, J Fedorko 1, M Birrer 1, G Evan 1, F Kaye 1, E Sausville 1, J Minna 1
PMCID: PMC365511  PMID: 3054516

Abstract

The human proto-oncogene L-myc generates at least four different mRNAs by alternative RNA processing. We have identified two phosphorylated L-myc proteins with molecular masses of 60,000 and 66,000 daltons [p60L-myc(human) and p66L-myc(human)] in a small-cell carcinoma line expressing high levels of L-myc mRNA. These proteins have a short half-life and are localized to the nuclear matrix fraction, as previously reported for the c-myc and N-myc proteins. In vitro translation experiments demonstrated that both the p60 and p66 species are encoded by a 3.9-kilobase (kb) mRNA which retains intron 1, while only the p60 protein is translated from a 3.6-kb L-myc mRNA which has had intron 1 removed. While L-myc proteins [p32L-myc(human) and p37L-myc(human)] could be synthesized in vitro from 2.2-kb mRNA templates, no such proteins were detected by immunoprecipitation in vivo. These observations suggest that alternative RNA processing of the L-myc transcript could play a role in determining the steady-state levels of the p60L-myc and p66L-myc proteins.

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Selected References

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