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SUMOylation Mediates the Nuclear Translocation and Signaling of the IGF-1 Receptor
KTH, School of Computer Science and Communication (CSC), Computational Biology, CB.
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2010 (English)In: Science Signaling, ISSN 1945-0877, E-ISSN 1937-9145, Vol. 3, no 108Article in journal (Refereed) Published
Abstract [en]

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-like elements and increased transcription in reporter assays. The SUMOylation sites of IGF-1R were identified as three evolutionarily conserved lysine residues-Lys(1025), Lys(1100), and Lys(1120)-in the beta subunit of the receptor. Mutation of these SUMO-1 sites abolished the ability of IGF-1R to translocate to the nucleus and activate transcription, but did not alter its kinase-dependent signaling. Thus, we demonstrate a SUMOylation-mediated mechanism of IGF-1R signaling that has potential implications for gene regulation.

Place, publisher, year, edition, pages
2010. Vol. 3, no 108
Keyword [en]
growth-factor receptor, insulin-receptor, tyrosine kinase, i receptor, chromatin immunoprecipitation, transcription factor, sumo-1, modification, proximity ligation, egf receptor, protein
Identifiers
URN: urn:nbn:se:kth:diva-19315DOI: 10.1126/scisignal.2000628ISI: 000275647700002Scopus ID: 2-s2.0-77951628921OAI: oai:DiVA.org:kth-19315DiVA: diva2:337362
Funder
Swedish eā€Science Research Center
Note
QC 20120329Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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