ArticleNucleic acids research1996
The cis-acting elements involved in endonucleolytic cleavage of the 3' UTR of human IGF-II mRNAs bind a 50 kDa protein.
Article in Nucleic acids research, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- The poly(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity.Molecular and cellular biology · 2000Article
- A polysomal ribonuclease involved in the destabilization of albumin mRNA is a novel member of the peroxidase gene family.RNA (New York, N.Y.) · 1998Article
- A conserved structural element in horse and mouse IGF2 genes binds a methylation sensitive factor.Nucleic acids research · 1998Article
- Growth-condition-dependent regulation of insulin-like growth factor II mRNA stability.The Biochemical journal · 1996Article
- Transcriptional regulation and biological significance of the insulin like growth factor II gene.Cell proliferationReview
- Mechanisms of endonuclease-mediated mRNA decay.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-specific cleavage of human insulin-like growth factor II mRNAs requires two cis-acting elements, I and II, that are both located in the 3' untranslated region and separated by almost 2 kb. These elements can interact and form a stable RNA-RNA stem structure. In this study we have initiated the investigation of transacting factors involved in the cleavage of IGF-II mRNAs. The products of the cleavage reaction accumulate in the cytoplasm, suggesting that cleavage occurs in this cellular compartment. By electrophoretic mobility shift assays, we have identified a cytoplasmic protein with an apparent molecular weight of 48-50 kDa, IGF-II cleavage unit binding protein (ICU-BP), that binds to the stem structure formed by interaction of parts of the cis-acting elements I and II. The binding is resistant to high K+ concentrations and is dependent on Mg2+. In addition, ICU-BP binding is dependent on the cell density and correlates inversely with the IGM-II mRNA levels. In vivo cross-linking data show that this protein is associated with IGF-II mRNAs in vivo.
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Registered trials
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