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Sang Dae Kim  (Kim SD) 1 Article
Obesity and Metabolism
Insulin Phosphorylates Tyrosine Residue 464 of Tub and Translocates Tubby into the Nucleus in HIRcB Cells
Jin Wook Kim, Hyeon Soo Kim, Sang Dae Kim, Jung Yul Park
Endocrinol Metab. 2014;29(2):163-168.   Published online June 26, 2014
DOI: https://doi.org/10.3803/EnM.2014.29.2.163
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  • 7 Web of Science
  • 6 Crossref
AbstractAbstract PDFPubReader   
Background

The tubby protein has a motif that might be relevant for its action in the insulin signaling pathway. Previous studies have indicated that tubby undergoes phosphorylation on tyrosine residues in response to several stimuli and is known to localize in the nucleus as well as in the plasma membrane. However, the relationship between phosphorylation and nuclear translocation is not well understood. Here, we report that insulin directly phosphorylates tubby, which translocates into the nucleus.

Methods

The effects of insulin on Tubby were performed with Western blot. The immunoprecipitation and confocal microscopy were performed to prove phosphorylation and nuclear translocation.

Results

Mutation study reveals that tyrosine residue 464 of tubby gene (Tub) is a phosphorylation site activated by insulin. In addition, major portions of tubby protein in the plasma membrane are translocated into the nucleus after insulin treatment. Tyrosine kinase inhibitor pretreatment blocked insulin-induced tubby translocation, suggesting that phosphorylation is important for nuclear translocation. Moreover, mutant tyrosine residue 464 did not translocate into the nucleus in respond to insulin. These findings demonstrate that insulin phosphorylates tyrosine residue 464 of Tub, and this event is important for insulin-induced tubby nuclear translocation.

Conclusion

Insulin phosphorylates tyrosine residue 464 of Tub and translocates tubby into the nuclei of HIRcB cells.

Citations

Citations to this article as recorded by  
  • Shuttling of cellular proteins between the plasma membrane and nucleus (Review)
    Hua-Chuan Zheng, Hua-Mao Jiang
    Molecular Medicine Reports.2021;[Epub]     CrossRef
  • Tubby-like Protein 2 regulates homogalacturonan biosynthesis in Arabidopsis seed coat mucilage
    Meng Wang, Zongchang Xu, Rana Imtiaz Ahmed, Yiping Wang, Ruibo Hu, Gongke Zhou, Yingzhen Kong
    Plant Molecular Biology.2019; 99(4-5): 421.     CrossRef
  • The Caenorhabditis elegans Tubby homolog dynamically modulates olfactory cilia membrane morphogenesis and phospholipid composition
    Danielle DiTirro, Alison Philbrook, Kendrick Rubino, Piali Sengupta
    eLife.2019;[Epub]     CrossRef
  • The tubby-like proteins kingdom in animals and plants
    Meng Wang, Zongchang Xu, Yingzhen Kong
    Gene.2018; 642: 16.     CrossRef
  • Articles in 'Endocrinology and Metabolism' in 2014
    Won-Young Lee
    Endocrinology and Metabolism.2015; 30(1): 47.     CrossRef
  • The Role of Foxo3 in Leydig Cells
    Young Suk Choi, Joo Eun Song, Byung Soo Kong, Jae Won Hong, Silvia Novelli, Eun Jig Lee
    Yonsei Medical Journal.2015; 56(6): 1590.     CrossRef
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