ArticleMolecular and cellular biology1999
Differentiation-induced internal translation of c-sis mRNA: analysis of the cis elements and their differentiation-linked binding to the hnRNP C protein.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.
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Who cites it
53 citing papers in PubMed, 1 synthesis or guideline pooled it, 100 citations in OpenAlex.
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- Proteomic analysis of polyribosomes identifies splicing factors as potential regulators of translation during mitosis.Nucleic acids research · 2017Article
- Protein Translation and Signaling in Human Eosinophils.Frontiers in medicine · 2017Review
- Hydrogen peroxide induces La cytoplasmic shuttling and increases hepatitis C virus internal ribosome entry site-dependent translation.The Journal of general virology · 2016Article
- Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.RNA (New York, N.Y.) · 2015Article
- Role of human heterogeneous nuclear ribonucleoprotein C1/C2 in dengue virus replication.Virology journal · 2015Article
- Cap-Independent Translation in Hematological Malignancies.Frontiers in oncology · 2015Review
- Establishment of chronic hepatitis C virus infection: translational evasion of oxidative defence.World journal of gastroenterology · 2014Review
- Alternative Mechanisms to Initiate Translation in Eukaryotic mRNAs.Comparative and functional genomics · 2012Article
- Translational regulation of the cell cycle: when, where, how and why?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Review
- Protein kinase CK1alphaLS promotes vascular cell proliferation and intimal hyperplasia.The American journal of pathology · 2010Article
- Translational symphony in (hnRNP) C major for APP.Nature structural & molecular biology · 2010Article
- Role of polypyrimidine tract binding protein in mediating internal initiation of translation of interferon regulatory factor 2 RNA.PloS one · 2009Article
- Cap-independent translation of human SP-A 5'-UTR variants: a double-loop structure and cis-element contribution.American journal of physiology. Lung cellular and molecular physiology · 2009Article
- A gastrin transcript expressed in gastrointestinal cancer cells contains an internal ribosome entry site.British journal of cancer · 2008Article
- Downregulation of hnRNP C1/C2 by siRNA sensitizes HeLa cells to various stresses.Molecular and cellular biochemistry · 2007Article
- A role for hnRNP C1/C2 and Unr in internal initiation of translation during mitosis.The EMBO journal · 2007Article
- Searching for IRES.RNA (New York, N.Y.) · 2006Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In previous reports we showed that the long 5' untranslated region (5' UTR) of c-sis, the gene encoding the B chain of platelet-derived growth factor, has translational modulating activity due to its differentiation-activated internal ribosomal entry site (D-IRES). Here we show that the 5' UTR contains three regions with a computer-predicted Y-shaped structure upstream of an AUG codon, each of which can confer some degree of internal translation by itself. In nondifferentiated cells, the entire 5' UTR is required for maximal basal IRES activity. The elements required for the differentiation-sensing ability (i.e., D-IRES) were mapped to a 630-nucleotide fragment within the central portion of the 5' UTR. Even though the region responsible for IRES activation is smaller, the full-length 5' UTR is capable of mediating the maximal translation efficiency in differentiated cells, since only the entire 5' UTR is able to confer the maximal basal IRES activity. Interestingly, a 43-kDa protein, identified as hnRNP C, binds in a differentiation-induced manner to the differentiation-sensing region. Using UV cross-linking experiments, we show that while hnRNP C is mainly a nuclear protein, its binding activity to the D-IRES is mostly nuclear in nondifferentiated cells, whereas in differentiated cells such binding activity is associated with the ribosomal fraction. Since the c-sis 5' UTR is a translational modulator in response to cellular changes, it seems that the large number of cross-talking structural entities and the interactions with regulated trans-acting factors are important for the strength of modulation in response to cellular changes. These characteristics may constitute the major difference between strong IRESs, such as those seen in some viruses, and IRESs that serve as translational modulators in response to developmental signals, such as that of c-sis.
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