Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation.
IGF2BP2 is a member of a family of mRNA binding proteins that, collectively, have been shown to bind to several different mRNAs in mammalian cells, including one of the mRNAs encoding insulin-like growth factor-2. Polymorphisms in the Igf2bp2 gene are associated with risk of developing type 2 diabet...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0033140&type=printable |
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| author | Hang T T Le Alice M Sorrell Kenneth Siddle |
| author_facet | Hang T T Le Alice M Sorrell Kenneth Siddle |
| author_sort | Hang T T Le |
| collection | DOAJ |
| description | IGF2BP2 is a member of a family of mRNA binding proteins that, collectively, have been shown to bind to several different mRNAs in mammalian cells, including one of the mRNAs encoding insulin-like growth factor-2. Polymorphisms in the Igf2bp2 gene are associated with risk of developing type 2 diabetes, but detailed functional characterisation of IGF2BP2 protein is lacking. By immunoblotting with C-terminally reactive antibodies we identified a novel IGF2BP2 isoform with a molecular weight of 58 kDa in both human and rodents, that is expressed at somewhat lower levels than the full-length 65 kDa protein. We demonstrated by mutagenesis that this isoform is generated by alternative translation initiation at the internal Met69. It lacks a conserved N-terminal RNA Recognition Motif (RRM) and would be predicted to differ functionally from the canonical full length isoform. We further investigated IGF2BP2 mRNA transcripts by amplification of cDNA using 5'-RACE. We identified multiple transcription start sites of the human, mouse and rat Igf2bp2 genes in a highly conserved region only 50-90 nts upstream of the major translation start site, ruling out the existence of N-terminally extended isoforms. We conclude that structural heterogeneity of IGF2BP2 protein should be taken into account when considering cellular function. |
| format | Article |
| id | doaj-art-7c75bb75adb8432d962fff1474fba3ec |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-7c75bb75adb8432d962fff1474fba3ec2025-08-20T02:05:35ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0173e3314010.1371/journal.pone.0033140Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation.Hang T T LeAlice M SorrellKenneth SiddleIGF2BP2 is a member of a family of mRNA binding proteins that, collectively, have been shown to bind to several different mRNAs in mammalian cells, including one of the mRNAs encoding insulin-like growth factor-2. Polymorphisms in the Igf2bp2 gene are associated with risk of developing type 2 diabetes, but detailed functional characterisation of IGF2BP2 protein is lacking. By immunoblotting with C-terminally reactive antibodies we identified a novel IGF2BP2 isoform with a molecular weight of 58 kDa in both human and rodents, that is expressed at somewhat lower levels than the full-length 65 kDa protein. We demonstrated by mutagenesis that this isoform is generated by alternative translation initiation at the internal Met69. It lacks a conserved N-terminal RNA Recognition Motif (RRM) and would be predicted to differ functionally from the canonical full length isoform. We further investigated IGF2BP2 mRNA transcripts by amplification of cDNA using 5'-RACE. We identified multiple transcription start sites of the human, mouse and rat Igf2bp2 genes in a highly conserved region only 50-90 nts upstream of the major translation start site, ruling out the existence of N-terminally extended isoforms. We conclude that structural heterogeneity of IGF2BP2 protein should be taken into account when considering cellular function.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0033140&type=printable |
| spellingShingle | Hang T T Le Alice M Sorrell Kenneth Siddle Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. PLoS ONE |
| title | Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. |
| title_full | Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. |
| title_fullStr | Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. |
| title_full_unstemmed | Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. |
| title_short | Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation. |
| title_sort | two isoforms of the mrna binding protein igf2bp2 are generated by alternative translational initiation |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0033140&type=printable |
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