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Volumn 6, Issue , 2015, Pages

SUMOylation of AMPKα1 by PIAS4 specifically regulates mTORC1 signalling

Author keywords

[No Author keywords available]

Indexed keywords

6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; AMP ACTIVATED PROTEIN KINASE ALPHA1; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; LIGASE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PIAS4 LIGASE; UNCLASSIFIED DRUG; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; PIAS4 PROTEIN, HUMAN; PRKAA1 PROTEIN, HUMAN; PROTEIN INHIBITOR OF ACTIVATED STAT; TARGET OF RAPAMYCIN KINASE;

EID: 84948753909     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9979     Document Type: Article
Times cited : (37)

References (58)
  • 1
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie, D. G., Ross, F. A. & Hawley, S. A. AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 13, 251-262 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 2
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova, M. M. & Shaw, R. J. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 13, 1016-1023 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 3
    • 3543025724 scopus 로고    scopus 로고
    • AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms
    • Xiang, X., Saha, A. K., Wen, R., Ruderman, N. B. & Luo, Z. AMP-activated protein kinase activators can inhibit the growth of prostate cancer cells by multiple mechanisms. Biochem. Biophys. Res. Commun. 321, 161-167 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 161-167
    • Xiang, X.1    Saha, A.K.2    Wen, R.3    Ruderman, N.B.4    Luo, Z.5
  • 4
    • 20144387628 scopus 로고    scopus 로고
    • Mimicry of a cellular low energy status blocks tumor cell anabolism and suppresses the malignant phenotype
    • Swinnen, J. V. et al. Mimicry of a cellular low energy status blocks tumor cell anabolism and suppresses the malignant phenotype. Cancer Res. 65, 2441-2448 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 2441-2448
    • Swinnen, J.V.1
  • 5
    • 33751284806 scopus 로고    scopus 로고
    • Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells
    • Zakikhani, M., Dowling, R., Fantus, I. G., Sonenberg, N. & Pollak, M. Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells. Cancer Res. 66, 10269-10273 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 10269-10273
    • Zakikhani, M.1    Dowling, R.2    Fantus, I.G.3    Sonenberg, N.4    Pollak, M.5
  • 6
    • 44449103256 scopus 로고    scopus 로고
    • Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice
    • Huang, X. et al. Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice. Biochem J. 412, 211-221 (2008).
    • (2008) Biochem J. , vol.412 , pp. 211-221
    • Huang, X.1
  • 7
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • Carling, D., Zammit, V. A. & Hardie, D. G. A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett. 223, 217-222 (1987).
    • (1987) FEBS Lett. , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 8
    • 67749111502 scopus 로고    scopus 로고
    • The LKB1-AMPK pathway: Metabolism and growth control in tumour suppression
    • Shackelford, D. B. & Shaw, R. J. The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. Nat. Rev. Cancer. 9, 563-575 (2009).
    • (2009) Nat. Rev. Cancer. , vol.9 , pp. 563-575
    • Shackelford, D.B.1    Shaw, R.J.2
  • 9
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T. & Guan, K. L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590 (2003).
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 10
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • Gwinn, D. M. et al. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol. Cell 30, 214-226 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.1
  • 11
    • 36048930364 scopus 로고    scopus 로고
    • Localization of AMP kinase is regulated by stress, cell density, and signaling through the MEK-4ERK1/2 pathway
    • Kodiha, M., Rassi, J. G., Brown, C. M. & Stochaj, U. Localization of AMP kinase is regulated by stress, cell density, and signaling through the MEK--4ERK1/2 pathway. Am. J. Physiol. Cell Physiol. 293, C1427-C1436 (2007).
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , pp. C1427-C1436
    • Kodiha, M.1    Rassi, J.G.2    Brown, C.M.3    Stochaj, U.4
  • 12
    • 77958066938 scopus 로고    scopus 로고
    • Identification of a nuclear export signal in the catalytic subunit of AMP-activated protein kinase
    • Kazgan, N., Williams, T., Forsberg, L. J. & Brenman, J. E. Identification of a nuclear export signal in the catalytic subunit of AMP-activated protein kinase. Mol. Biol. Cell 21, 3433-3442 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3433-3442
    • Kazgan, N.1    Williams, T.2    Forsberg, L.J.3    Brenman, J.E.4
  • 13
    • 13344285343 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase subfamily
    • Stapleton, D. et al. Mammalian AMP-activated protein kinase subfamily. J. Biol. Chem. 271, 611-614 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 611-614
    • Stapleton, D.1
  • 14
    • 0032529139 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform
    • Salt, I. et al. AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform. Biochem. J. 334 (Pt 1), 177-187 (1998).
    • (1998) Biochem. J. , vol.334 , pp. 177-187
    • Salt, I.1
  • 15
    • 0030592623 scopus 로고    scopus 로고
    • The alpha1 and alpha2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • Woods, A., Salt, I., Scott, J., Hardie, D. G. & Carling, D. The alpha1 and alpha2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Lett. 397, 347-351 (1996).
    • (1996) FEBS Lett. , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5
  • 16
    • 78650606464 scopus 로고    scopus 로고
    • B-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK)
    • Oakhill, J. S. et al. b-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK). Proc. Natl Acad. Sci. USA 107, 19237-19241 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19237-19241
    • Oakhill, J.S.1
  • 17
    • 84903627732 scopus 로고    scopus 로고
    • Gain-of-function mutant p53 promotes cell growth and cancer cell metabolism via inhibition of AMPK activation
    • Zhou, G. et al. Gain-of-function mutant p53 promotes cell growth and cancer cell metabolism via inhibition of AMPK activation. Mol. Cell 54, 960-974 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 960-974
    • Zhou, G.1
  • 18
    • 84875895286 scopus 로고    scopus 로고
    • Alpha-SNAP inhibits AMPK signaling to reduce mitochondrial biogenesis and dephosphorylates Thr172 in AMPK alpha in vitro
    • Wang, L. & Brautigan, D. L. alpha-SNAP inhibits AMPK signaling to reduce mitochondrial biogenesis and dephosphorylates Thr172 in AMPK alpha in vitro. Nat. Commun. 4, 1559 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1559
    • Wang, L.1    Brautigan, D.L.2
  • 19
    • 84887189624 scopus 로고    scopus 로고
    • Inhibition of AMPK catabolic action by GSK3
    • Suzuki, T. et al. Inhibition of AMPK catabolic action by GSK3. Mol. Cell 50, 407-419 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 407-419
    • Suzuki, T.1
  • 20
    • 84874077399 scopus 로고    scopus 로고
    • E3 ubiquitin ligase, WWP1, interacts with AMPKalpha2 and down-regulates its expression in skeletal muscle C2C12 cells
    • Lee, J. O. et al. E3 ubiquitin ligase, WWP1, interacts with AMPKalpha2 and down-regulates its expression in skeletal muscle C2C12 cells. J. Biol. Chem. 288, 4673-4680 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 4673-4680
    • Lee, J.O.1
  • 21
    • 44649099112 scopus 로고    scopus 로고
    • Downregulation of AMP-activated protein kinase by Cideamediated ubiquitination and degradation in brown adipose tissue
    • Qi, J. et al. Downregulation of AMP-activated protein kinase by Cideamediated ubiquitination and degradation in brown adipose tissue. EMBO J. 27, 1537-1548 (2008).
    • (2008) EMBO J. , vol.27 , pp. 1537-1548
    • Qi, J.1
  • 22
    • 70350359685 scopus 로고    scopus 로고
    • KSR2 is an essential regulator of AMP kinase, energy expenditure, and insulin sensitivity
    • Costanzo-Garvey, D. L. et al. KSR2 is an essential regulator of AMP kinase, energy expenditure, and insulin sensitivity. Cell Metab. 10, 366-378 (2009).
    • (2009) Cell Metab. , vol.10 , pp. 366-378
    • Costanzo-Garvey, D.L.1
  • 23
    • 48449101433 scopus 로고    scopus 로고
    • P53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling
    • Budanov, A. V. & Karin, M. p53 target genes sestrin1 and sestrin2 connect genotoxic stress and mTOR signaling. Cell 134, 451-460 (2008).
    • (2008) Cell , vol.134 , pp. 451-460
    • Budanov, A.V.1    Karin, M.2
  • 24
    • 80052939858 scopus 로고    scopus 로고
    • Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction
    • Lu, J. Y. et al. Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction. Cell 146, 969-979 (2011).
    • (2011) Cell , vol.146 , pp. 969-979
    • Lu, J.Y.1
  • 25
    • 84886409705 scopus 로고    scopus 로고
    • SUM Oylation regulates the SNF1 protein kinase
    • Simpson-Lavy, K. J. & Johnston, M. SUM Oylation regulates the SNF1 protein kinase. Proc. Natl Acad. Sci. USA 110, 17432-17437 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 17432-17437
    • Simpson-Lavy, K.J.1    Johnston, M.2
  • 26
    • 79960326517 scopus 로고    scopus 로고
    • Ubp8 and SAGA regulate Snf1 AMP kinase activity
    • Wilson, M. A. et al. Ubp8 and SAGA regulate Snf1 AMP kinase activity. Mol. Cell Biol. 31, 3126-3135 (2011).
    • (2011) Mol. Cell Biol. , vol.31 , pp. 3126-3135
    • Wilson, M.A.1
  • 27
    • 42449090346 scopus 로고    scopus 로고
    • Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains
    • Al-Hakim, A. K. et al. Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains. Biochem. J. 411, 249-260 (2008).
    • (2008) Biochem. J. , vol.411 , pp. 249-260
    • Al-Hakim, A.K.1
  • 28
    • 84922689340 scopus 로고    scopus 로고
    • Degradation of AMPK by a cancer-specific ubiquitin ligase
    • Pineda, C. T. et al. Degradation of AMPK by a cancer-specific ubiquitin ligase. Cell 160, 715-728 (2015).
    • (2015) Cell , vol.160 , pp. 715-728
    • Pineda, C.T.1
  • 29
    • 33747071284 scopus 로고    scopus 로고
    • TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase
    • Solaz-Fuster, M. C., Gimeno-Alcaniz, J. V., Casado, M. & Sanz, P. TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase. Cell Signal. 18, 1702-1712 (2006).
    • (2006) Cell Signal. , vol.18 , pp. 1702-1712
    • Solaz-Fuster, M.C.1    Gimeno-Alcaniz, J.V.2    Casado, M.3    Sanz, P.4
  • 30
    • 84355161919 scopus 로고    scopus 로고
    • Chemical genetic screen for AMPKalpha2 substrates uncovers a network of proteins involved in mitosis
    • Banko, M. R. et al. Chemical genetic screen for AMPKalpha2 substrates uncovers a network of proteins involved in mitosis. Mol. Cell 44, 878-892 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 878-892
    • Banko, M.R.1
  • 32
    • 85047689953 scopus 로고
    • 5-aminoimidazole- 4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?
    • Corton, J. M., Gillespie, J. G., Hawley, S. A. & Hardie, D. G. 5-aminoimidazole- 4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells? Eur. J. Biochem. 229, 558-565 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 33
    • 21344432585 scopus 로고    scopus 로고
    • Disruption of the murine PIASx gene results in reduced testis weight
    • Santti, H. et al. Disruption of the murine PIASx gene results in reduced testis weight. J. Mol. Endocrinol. 34, 645-654 (2005).
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 645-654
    • Santti, H.1
  • 34
    • 77955287742 scopus 로고    scopus 로고
    • Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner
    • Kalender, A. et al. Metformin, independent of AMPK, inhibits mTORC1 in a rag GTPase-dependent manner. Cell Metab. 11, 390-401 (2010).
    • (2010) Cell Metab. , vol.11 , pp. 390-401
    • Kalender, A.1
  • 35
    • 84878695660 scopus 로고    scopus 로고
    • Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity
    • Rubio, T., Vernia, S. & Sanz, P. Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity. Mol. Biol. Cell. 24, 1801-1811, S1801-S1804 (2013).
    • (2013) Mol. Biol. Cell. , vol.24 , Issue.1801-1811 , pp. S1801-S1804
    • Rubio, T.1    Vernia, S.2    Sanz, P.3
  • 36
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante, M. & Sabatini, D. M. mTOR signaling in growth control and disease. Cell 149, 274-293 (2012).
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 37
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P. & Snyder, S. H. RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78, 35-43 (1994).
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 38
    • 0024839973 scopus 로고
    • Tissue distribution of the AMPactivated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • Davies, S. P., Carling, D. & Hardie, D. G. Tissue distribution of the AMPactivated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. Eur. J. Biochem. 186, 123-128 (1989).
    • (1989) Eur. J. Biochem. , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 39
    • 33745210316 scopus 로고    scopus 로고
    • The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis
    • Bischof, O. et al. The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis. Mol. Cell 22, 783-794 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 783-794
    • Bischof, O.1
  • 40
    • 33751252292 scopus 로고    scopus 로고
    • Direct observation of individual endogenous protein complexes in situ by proximity ligation
    • Soderberg, O. et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat. Methods 3, 995-1000 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 995-1000
    • Soderberg, O.1
  • 41
    • 84904459334 scopus 로고    scopus 로고
    • Effects of metformin on breast cancer cell proliferation, the AMPK pathway and the cell cycle
    • Hadad, S. M., Hardie, D. G., Appleyard, V. & Thompson, A. M. Effects of metformin on breast cancer cell proliferation, the AMPK pathway and the cell cycle. Clin. Transl. Oncol. 16, 746-752 (2014).
    • (2014) Clin. Transl. Oncol. , vol.16 , pp. 746-752
    • Hadad, S.M.1    Hardie, D.G.2    Appleyard, V.3    Thompson, A.M.4
  • 42
    • 33744514139 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome
    • Cool, B. et al. Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. Cell Metab. 3, 403-416 (2006).
    • (2006) Cell Metab. , vol.3 , pp. 403-416
    • Cool, B.1
  • 43
    • 84890963021 scopus 로고    scopus 로고
    • Structural basis of AMPK regulation by small molecule activators
    • Xiao, B. et al. Structural basis of AMPK regulation by small molecule activators. Nat. Commun. 4, 3017 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 3017
    • Xiao, B.1
  • 44
    • 84901329684 scopus 로고    scopus 로고
    • Small molecule drug A-769662 and AMP synergistically activate naive AMPK independent of upstream kinase signaling
    • Scott, J. W. et al. Small molecule drug A-769662 and AMP synergistically activate naive AMPK independent of upstream kinase signaling. Chem. Biol. 21, 619-627 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 619-627
    • Scott, J.W.1
  • 45
    • 1042267229 scopus 로고    scopus 로고
    • Determinants of rapamycin sensitivity in breast cancer cells
    • Noh, W. C. et al. Determinants of rapamycin sensitivity in breast cancer cells. Clin. Cancer Res. 10, 1013-1023 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 1013-1023
    • Noh, W.C.1
  • 46
    • 69149097363 scopus 로고    scopus 로고
    • The AMPK agonist AICAR inhibits the growth of EGFRvIIIexpressing glioblastomas by inhibiting lipogenesis
    • Guo, D. et al. The AMPK agonist AICAR inhibits the growth of EGFRvIIIexpressing glioblastomas by inhibiting lipogenesis. Proc. Natl Acad. Sci. USA 106, 12932-12937 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 12932-12937
    • Guo, D.1
  • 47
    • 84892933078 scopus 로고    scopus 로고
    • Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity
    • Houde, V. P. et al. Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity. Biochem. J. 458, 4156 (2014).
    • (2014) Biochem. J. , vol.458 , pp. 41-56
    • Houde, V.P.1
  • 48
    • 79961116788 scopus 로고    scopus 로고
    • Nuclear translocation of AMPK-alpha1 potentiates striatal neurodegeneration in Huntingtons disease
    • Ju, T. C. et al. Nuclear translocation of AMPK-alpha1 potentiates striatal neurodegeneration in Huntingtons disease. J. Cell Biol. 194, 209-227 (2011).
    • (2011) J. Cell Biol. , vol.194 , pp. 209-227
    • Ju, T.C.1
  • 49
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R. T. SUMO: a history of modification. Mol. Cell 18, 1-12 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 50
    • 59249108098 scopus 로고    scopus 로고
    • SUMOylation inhibits SF-1 activity by reducing CDK7- mediated serine 203 phosphorylation
    • Yang, W. H. et al. SUMOylation inhibits SF-1 activity by reducing CDK7- mediated serine 203 phosphorylation. Mol. Cell. Biol. 29, 613-625 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 613-625
    • Yang, W.H.1
  • 51
    • 84885168009 scopus 로고    scopus 로고
    • AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation
    • Gowans, G. J., Hawley, S. A., Ross, F. A. & Hardie, D. G. AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation. Cell Metab. 18, 556-566 (2013).
    • (2013) Cell Metab. , vol.18 , pp. 556-566
    • Gowans, G.J.1    Hawley, S.A.2    Ross, F.A.3    Hardie, D.G.4
  • 52
    • 70350031566 scopus 로고    scopus 로고
    • SUMOylation attenuates the function of PGC-1alpha
    • Rytinki, M. M. & Palvimo, J. J. SUMOylation attenuates the function of PGC-1alpha. J. Biol. Chem. 284, 26184-26193 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 26184-26193
    • Rytinki, M.M.1    Palvimo, J.J.2
  • 54
    • 0033525191 scopus 로고    scopus 로고
    • A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins
    • Moilanen, A. M. et al. A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins. J. Biol. Chem. 274, 3700-3704 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3700-3704
    • Moilanen, A.M.1
  • 55
    • 33646033137 scopus 로고    scopus 로고
    • A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen
    • Moffat, J. et al. A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen. Cell 124, 1283-1298 (2006).
    • (2006) Cell , vol.124 , pp. 1283-1298
    • Moffat, J.1
  • 56
    • 75049085233 scopus 로고    scopus 로고
    • PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis
    • Djouder, N. et al. PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis. EMBO J. 29, 469-481 (2010).
    • (2010) EMBO J. , vol.29 , pp. 469-481
    • Djouder, N.1
  • 57
    • 0031464542 scopus 로고    scopus 로고
    • Induction of TNF-sensitive cellular phenotype by c-Myc involves p53 and impaired NF-kappaB activation
    • Klefstrom, J. et al. Induction of TNF-sensitive cellular phenotype by c-Myc involves p53 and impaired NF-kappaB activation. EMBO J. 16, 7382-7392 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7382-7392
    • Klefstrom, J.1
  • 58
    • 0029043548 scopus 로고
    • Site-specific recombination mediated by an adenovirus vector expressing the Cre recombinase protein: A molecular switch for control of gene expression
    • Anton, M. & Graham, F. L. Site-specific recombination mediated by an adenovirus vector expressing the Cre recombinase protein: a molecular switch for control of gene expression. J. Virol. 69, 4600-4606 (1995).
    • (1995) J. Virol. , vol.69 , pp. 4600-4606
    • Anton, M.1    Graham, F.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.