Unknown,Transcriptomics,Genomics,Proteomics

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Genome-wide analysis of insulin-like growth factor 1 receptor (IGF1R) binding sites in DFB cells


ABSTRACT: The insulin-like growth factor 1 receptor (IGF-1R) plays crucial roles in developmental and cancer biology. Most of its biological effects have been ascribed to its tyrosine kinase activity. We report that IGF-1 promotes the modification of IGF-1R by small ubiquitin-like modifier protein-1 (SUMO-1) and its translocation to the nucleus. Nuclear IGF-1R associated with enhancer-like elements and increased transcription in reporter assays. We used ChIP-seq to examine the interaction of IGF-1R with DNA on a genome-wide scale. Analysis of the data set resulted in 568 candidate peaks, that is, statistically significant IGF-1R-enriched regions. The IGF-1R-enriched regions were divided into five classes on the basis of their location relative to known genes. Most of the IGF-1R-interacting sites (80%) were located distal from any annotated gene (intergenic), 6.3% were located in introns, 6.3% in exons, 3.4% were <20 kb upstream of an annotated transcript start site (5'UTR + 20 kb upstream), and 3.6% were <20 kb downstream of an annotated transcript end site (3'UTR + 20 kb downstream). Analysis of the genomic interaction of IGF1R in DFB cells

ORGANISM(S): Homo sapiens

SUBMITTER: Ali Tofigh 

PROVIDER: E-GEOD-23792 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

SUMOylation mediates the nuclear translocation and signaling of the IGF-1 receptor.

Sehat Bita B   Tofigh Ali A   Lin Yingbo Y   Trocmé Eric E   Liljedahl Ulrika U   Lagergren Jens J   Larsson Olle O  

Science signaling 20100209 108


The insulin-like growth factor 1 receptor (IGF-1R) plays crucial roles in developmental and cancer biology. Most of its biological effects have been ascribed to its tyrosine kinase activity, which propagates signaling through the phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways. Here, we report that IGF-1 promotes the modification of IGF-1R by small ubiquitin-like modifier protein-1 (SUMO-1) and its translocation to the nucleus. Nuclear IGF-1R associated with enhancer-  ...[more]

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