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| Screening of AMPK Interacted Proteins by Yeast Two Hybrid System |
| WU Li1, YANG Cheng-hong1, DENG Si-si2, ZHOU Yu-bo2, QIAN Min1, ZANG Yi2 |
1. School of Life Science, East China Normal University, Shanghai 200062, China;
2. The National Center for Drug Screening, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China |
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Abstract Adenosine Monophosphate-activated protein kinase (AMP-activated protein kinase, AMPK), a serine/threonine protein kinase, regulates cellular energy homeostasis. Based on yeast two hybrid assay,63 proteins identified interacted with AMPK β1 subunit in the human universal cDNA library. Among these proteins, there are 30 enzymes including metabolic enzymes, kinases and SUMO protease, 9 transcription factors or their coregulators, 5 transport/cargo proteins, 4 GTP-binding proteins, 3 adaptors and some proteins involved in cell cycle, DNA repair and cell growth and/or maintainance. These results suggested that AMPK may play a key role not only in the metabolism but also in non-metabolism processes in the cellular functions.
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Received: 28 October 2011
Published: 25 February 2012
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[1] Carling D. AMP-activated protein kinase: balancing the scales. Biochimie, 2005, 87: 87-91.
[2] Leff T. AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins. Biochem Soc Trans, 2003, 31: 224-227.
[3] Hardie D G. AMP-activated/SNF1protein kinases: conserved guardians of cellular energy. Nature, 2007, 8: 774-785.
[4] McBride A, Ghilagaber S, Nikolaew A, et al. The glycogen-bingding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab, 2009, 9: 23-34.
[5] Warden S M, Richardson C, O'Donnell J, et al. Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization. Biochem J, 2001, 354(Pt 2): 275-283.
[6] Scott J W, Hawley S A, Green K A, et al. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J Clin Invest, 2004, 113(2): 274-284.
[7] Wu Y, Song P, Xu J, et al. Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J Biol Chem, 2007, 282: 9777-9788.
[8] Djouder N, Tuerk R D, Sulvioni P, et al. PKA phosphorylates and inactivates AMPK alpha to promote efficient lipolysis. EMBO J, 2010, 29(2): 469-481.
[9] Mitchelhill K I, Stapleton K, Gao G, et al. Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J Biol Chem, 1994, 296 (4):2361-2364.
[10] Leclerc I, Viollet B, Xavierda S, et al. Role of AMP-activated protein kinase in the regulation of gene transcription. Biochem Soc Trans, 2002, 30: 307-311.
[11] Horman S, Browne G, Krause U, et al. Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and inhibition of protein synthesis. Curr Biol, 2002, 12: 1419-1423.
[12] Lim C T, Kola B, Korbonits M. AMPK as a mediator of hormonal signaling. Journal of Mol Endocrinol, 2010, 44: 87-97.
[13] Stapleton D, Mitchilhill K I, Gao G, et al. Mammalian AMP-activated protein kinase subfamily. J Biol Chem, 1996, 271: 611-914.
[14] Chen Z, Heierhorst J, Mann R J, et al. Expression of the AMP-activated protein kinase β1 and β2 subunits in skeletal muscle. FEBS Lett, 1999, 460: 343-348.
[15] Mahiapuu M, Johansson C, Lindgren K, et al. Expression profiling of the γ-subunit isoforms of AMP-activated protein kinase suggests a major role for γ3 in white skeletal muscle. Am J Physiol Endocrinol Metab, 2004, 286:194-200.
[16] Moreno D, Viana R, Sanz P. Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase. Int J Biochem Cell Biol, 2009, 41(12): 2431-2439.
[17] Song H, Guan Y, Zhang L, et al. SPARC interacts with AMPK and regulates GLUT4 expression. Biochem Biophys Res Commun, 2010, 396 (4): 961-966.
[18] Stagljar I, Fields S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem Sci, 2002, 27:559-563.
[19] Uetz P, Giot L, Cagney G, et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 2000, 403(6770): 623-627.
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