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The function study on the interaction between Grb2 and AMPK

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Abstract

Growth factor receptor-bound protein 2 (Grb2) is an extensively studied adaptor protein involved in cell signaling. Grb2 is a highly flexible protein composed of a single SH2 domain flanked by two SH3 domains. The evolutionarily conserved serine/threonine kinase, AMP-activated protein kinase (AMPK), functions as a cellular fuel gauge that regulates metabolic pathways in glucose and fatty acid metabolism and protein synthesis. AMPK regulates the activation of TSC2 by phosphorylating TSC2. Here we report for the first time on the interaction of Grb2 with AMPK. SH2 domain of Grb2 and KIS domain of AMPK are both required for the combination of Grb2 and AMPK. Furthermore, Grb2 function as a factor which mediates phosphorylation of AMPK at Thr172, and potentially involves in metabolism pathways and AMPK-TSC2-mTOR cell growth pathway through regulating the activation of AMPK.

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Acknowledgments

We are grateful to Dr. Yi Tie for providing the Akt1 plasmid. This work was partially supported by Chinese National Natural Science Foundation Projects (30600123, 30621063) and Chinese National Basic Research Program (2006CB910802).

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Authors and Affiliations

  1. State Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, Beijing, 100850, China

    Zhi Pan, Jian Wang, Xiushan Yin, Ping Xie, Juntao Yang, Lingqiang Zhang & Fuchu He

  2. College of Life Science, Hebei University, Baoding, 071002, China

    Zhi Pan & Jizhi Jiang

  3. College of Life Science, Shandong Normal University, Jinan, 250014, China

    Ping Xie

  4. Institute of Biomedical Sciences, Fudan University, Shanghai, 200032, China

    Fuchu He

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  1. Zhi Pan
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  2. Jian Wang
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  3. Xiushan Yin
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  5. Juntao Yang
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Correspondence to Lingqiang Zhang or Fuchu He.

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Pan, Z., Wang, J., Yin, X. et al. The function study on the interaction between Grb2 and AMPK. Mol Cell Biochem 307, 121–127 (2008). https://doi.org/10.1007/s11010-007-9591-6

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  • DOI: https://doi.org/10.1007/s11010-007-9591-6

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