Colocalization and identification of interaction sites between IGFBP-3 and GalNAc-T14

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• 作者：Chen Wu^a ; ^{dawnwuchen@163.com} ; Si-Si Ma^b ; Jian-Feng Ge^c ; Yuan-Yuan Wang^a ; Huan-Na Tian^a ; Xiao-Bo Liu^d ; Bo Zhang^a ; Fang-Ming Liu^a ; Xiao-Kang Zhang^a ; Qin-Jian Li^a
• 关键词：IGFBP-3 ; Insulin-like growth factor binding protein 3 ; IGFBP ; Insulin-like growth factor binding protein ; GalNAc-T14 ; N-acetylgalactosaminyltransferase 14 ; GalNAc-Tases ; N-acetylgalactosaminyltransferases ; IGF-independent ; Insulin-like growth factor-indep
• 刊名：Gene
• 出版年：2012
• 期刊代码：73_03781119
• 类别：bio
• 出版时间：15 May, 2012
• 卷：499
• 期：2
• 页码：347-351
• 文件大小：595 K

摘要

GalNAc-T14 was identified as a novel IGFBP-3 binding partner in previous studies. Here, we furtherly confirmed the interaction between them by confocal microscopy, and identified the binding domain and probable interaction sites of GalNAc-T14 with IGFBP-3. The result of subcellular localization indicated that GalNAc-T14 was distributed in the cytosol, whereas IGFBP-3 existed in the cytosol and nucleolus. Confocal analyses demonstrated that IGFBP-3 and GalNAc-T14 colocalized in the cytosol. The result from yeast two hybrid assay showed that the C terminus of GalNAc-T14 (408-552aa) was essential for the interaction between GalNAc-T14 and IGFBP-3, especially Tyr⁴⁰⁸, Pro⁴⁰⁹, and Glu⁴¹⁰ of GalNAc-T14 may play key roles in the interaction with IGFBP-3. In conclusion, these studies demonstrated that IGFBP-3 and GalNAc-T14 are colocalized in MCF-7 cells and confirmed the interaction between IGFBP-3 and GalNAc-T14. This interaction may play an important role in the functional regulation of IGFBP-3.