2003
DOI: 10.1210/en.2002-220798
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Phosphorylation of Insulin-Like Growth Factor Binding Protein-3 by Deoxyribonucleic Acid-Dependent Protein Kinase Reduces Ligand Binding and Enhances Nuclear Accumulation

Abstract: The IGF binding proteins (IGFBPs) regulate the mitogenic effects of IGFs in the extracellular environment. Several members of this family, including IGFBP-3, also appear to have IGF-independent effects on cell function. For IGFBP-3 and IGFBP-5, both of which are translocated to the cell nuclei, these effects may be related to their putative nuclear actions. Because reversible phosphorylation is an important mechanism for controlling nuclear protein import, we have examined the effect of phosphorylating IGFBP-3… Show more

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Cited by 50 publications
(53 citation statements)
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“…The mechanism involves interaction with Importin Beta (Schedlich et al, 2003), a gene not previously recognised to be regulated by hypoxia, which was induced by hypoxia in our study (4.1-fold) in vitro. Thus, induction of IGFBP3 may have a more complex role then previously reported.…”
Section: Discussionsupporting
confidence: 47%
See 1 more Smart Citation
“…The mechanism involves interaction with Importin Beta (Schedlich et al, 2003), a gene not previously recognised to be regulated by hypoxia, which was induced by hypoxia in our study (4.1-fold) in vitro. Thus, induction of IGFBP3 may have a more complex role then previously reported.…”
Section: Discussionsupporting
confidence: 47%
“…In contrast to its extracellular IGF-binding role, an intracellular role of IGFBP-3 has been described (Schedlich et al, 2003), with phosphorylation increasing nuclear import of IGFBP-3, with release of IGF. The mechanism involves interaction with Importin Beta (Schedlich et al, 2003), a gene not previously recognised to be regulated by hypoxia, which was induced by hypoxia in our study (4.1-fold) in vitro.…”
Section: Discussionmentioning
confidence: 99%
“…IGFBP-5 nuclear localization has been reported in human breast carcinoma cell lines, 27 Chinese hamster ovary cells, 33 and porcine vascular smooth muscle cells. 34 We previously reported nuclear localization of IGFBP-5 in primary fibroblasts from fibrotic lung tissues, but not those from normal tissues. 17 We now show that IGFBP-5 translocates to the nucleus of IGFBP-5-expressing cells in a time-dependent manner.…”
Section: Discussionmentioning
confidence: 90%
“…It has been reported that human vitamin D receptor is phosphorylated at Ser 182 leading to an attenuation of its transactivation activity (43). Phosphorylation of IGFBP-3 has been shown to be involved in its nuclear translocation as well (44). By searching for the potential phosphorylation sites using the NetPhos 2.0 server (www.cbs.…”
Section: Discussionmentioning
confidence: 99%