메뉴 건너뛰기




Volumn 42, Issue 10, 2010, Pages 1729-1735

Phosphorylation of the von Hippel-Lindau protein (VHL) by protein kinase CK2 reduces its protein stability and affects p53 and HIF-1α mediated transcription

Author keywords

Degradation; HIF 1 ; P53; Protein kinase CK2; VHL tumour suppressor

Indexed keywords

4,5,6,7 TETRABROMOBENZOTRIAZOLE; CASEIN KINASE II; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROTEIN KINASE INHIBITOR; PROTEIN P53; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 77956187680     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.07.008     Document Type: Article
Times cited : (36)

References (27)
  • 2
    • 0028861059 scopus 로고
    • Mapping of the interaction sites of the growth suppressor protein p53 with the regulatory β-subunit of protein kinase CK2
    • Appel K., Wagner P., Boldyreff B., Issinger O.-G., Montenarh M. Mapping of the interaction sites of the growth suppressor protein p53 with the regulatory β-subunit of protein kinase CK2. Oncogene 1995, 11:1971-1978.
    • (1995) Oncogene , vol.11 , pp. 1971-1978
    • Appel, K.1    Wagner, P.2    Boldyreff, B.3    Issinger, O.-G.4    Montenarh, M.5
  • 3
    • 0037043777 scopus 로고    scopus 로고
    • Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis
    • Channavajhala P., Seldin D.C. Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene 2002, 21:5280-5288.
    • (2002) Oncogene , vol.21 , pp. 5280-5288
    • Channavajhala, P.1    Seldin, D.C.2
  • 4
    • 0034799401 scopus 로고    scopus 로고
    • Phosphorylation of Bid by casein kinases I and II regulates its cleavage by caspase 8
    • Desagher S., Osen-Sand A., Montessuit S., Magnenat E., Vilbois F., Hochmann A., et al. Phosphorylation of Bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell 2001, 8:601-611.
    • (2001) Mol Cell , vol.8 , pp. 601-611
    • Desagher, S.1    Osen-Sand, A.2    Montessuit, S.3    Magnenat, E.4    Vilbois, F.5    Hochmann, A.6
  • 6
    • 0043037839 scopus 로고    scopus 로고
    • Protein kinase CK2 binds to a multi-protein binding domain of the growth suppressor protein p53
    • Götz C., Scholtes P., Schuster N., Prowald A., Nastainczyk W., Montenarh M. Protein kinase CK2 binds to a multi-protein binding domain of the growth suppressor protein p53. Mol Cell Biochem 1999, 191:111-120.
    • (1999) Mol Cell Biochem , vol.191 , pp. 111-120
    • Götz, C.1    Scholtes, P.2    Schuster, N.3    Prowald, A.4    Nastainczyk, W.5    Montenarh, M.6
  • 7
    • 33746472918 scopus 로고    scopus 로고
    • Priming-dependent phosphorylation and regulation of the tumor suppressor pVHL by glycogen synthase kinase 3
    • Hergovich A., Lisztwan J., Thoma C.R., Wirbelauer C., Barry R.E., Krek W. Priming-dependent phosphorylation and regulation of the tumor suppressor pVHL by glycogen synthase kinase 3. Mol Cell Biol 2006, 26:5784-5796.
    • (2006) Mol Cell Biol , vol.26 , pp. 5784-5796
    • Hergovich, A.1    Lisztwan, J.2    Thoma, C.R.3    Wirbelauer, C.4    Barry, R.E.5    Krek, W.6
  • 8
    • 33748767112 scopus 로고    scopus 로고
    • Casein kinase 2 inhibition decreases hypoxia-inducible factor-1 activity under hypoxia through elevated p53 protein level
    • Hubert A., Paris S., Piret J.P., Ninane N., Raes M., Michiels C. Casein kinase 2 inhibition decreases hypoxia-inducible factor-1 activity under hypoxia through elevated p53 protein level. J Cell Sci 2006, 119:3351-3362.
    • (2006) J Cell Sci , vol.119 , pp. 3351-3362
    • Hubert, A.1    Paris, S.2    Piret, J.P.3    Ninane, N.4    Raes, M.5    Michiels, C.6
  • 9
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin W.G. Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer 2002, 2:673-682.
    • (2002) Nat Rev Cancer , vol.2 , pp. 673-682
    • Kaelin, W.G.1
  • 10
    • 0035868277 scopus 로고    scopus 로고
    • Perivenous expression of the mRNA of the three hypoxia-inducible factor alpha-subunits, HIF1alpha, HIF2alpha and HIF3alpha, in rat liver
    • Kietzmann T., Cornesse Y., Brechtel K., Modaressi S., Jungermann K. Perivenous expression of the mRNA of the three hypoxia-inducible factor alpha-subunits, HIF1alpha, HIF2alpha and HIF3alpha, in rat liver. Biochem J 2001, 354:531-537.
    • (2001) Biochem J , vol.354 , pp. 531-537
    • Kietzmann, T.1    Cornesse, Y.2    Brechtel, K.3    Modaressi, S.4    Jungermann, K.5
  • 11
    • 16644373473 scopus 로고    scopus 로고
    • Role of VHL gene mutation in human cancer
    • Kim W.Y., Kaelin W.G. Role of VHL gene mutation in human cancer. J Clin Oncol 2004, 22:4991-5004.
    • (2004) J Clin Oncol , vol.22 , pp. 4991-5004
    • Kim, W.Y.1    Kaelin, W.G.2
  • 12
    • 0035884195 scopus 로고    scopus 로고
    • Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1
    • Krippner-Heidenreich A., Talanian R.V., Sekul R., Kraft R., Thole H., Ottleben H., et al. Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem J 2001, 358:705-715.
    • (2001) Biochem J , vol.358 , pp. 705-715
    • Krippner-Heidenreich, A.1    Talanian, R.V.2    Sekul, R.3    Kraft, R.4    Thole, H.5    Ottleben, H.6
  • 14
    • 0011721856 scopus 로고
    • Monoclonal antibody analysis of the SV40 large T antigen-p53 complex
    • Lane D.P., Gannon J.V. Monoclonal antibody analysis of the SV40 large T antigen-p53 complex. Cancer Cells 1986, 4:387-393.
    • (1986) Cancer Cells , vol.4 , pp. 387-393
    • Lane, D.P.1    Gannon, J.V.2
  • 15
    • 0030477012 scopus 로고    scopus 로고
    • Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes
    • Lohrum M., Scheidtmann K.H. Differential effects of phosphorylation of rat p53 on transactivation of promoters derived from different p53 responsive genes. Oncogene 1996, 13:2527-2539.
    • (1996) Oncogene , vol.13 , pp. 2527-2539
    • Lohrum, M.1    Scheidtmann, K.H.2
  • 16
    • 20444457555 scopus 로고    scopus 로고
    • Tumor suppression by the von Hippel-Lindau protein requires phosphorylation of the acidic domain
    • Lolkema M.P., Gervais M.L., Snijckers C.M., Hill R.P., Giles R.H., Voest E.E., et al. Tumor suppression by the von Hippel-Lindau protein requires phosphorylation of the acidic domain. J Biol Chem 2005, 280:22205-22211.
    • (2005) J Biol Chem , vol.280 , pp. 22205-22211
    • Lolkema, M.P.1    Gervais, M.L.2    Snijckers, C.M.3    Hill, R.P.4    Giles, R.H.5    Voest, E.E.6
  • 17
    • 0033059744 scopus 로고    scopus 로고
    • Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable
    • McKendrick L., Milne D., Meek D. Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable. Mol Cell Biochem 1999, 191:187-199.
    • (1999) Mol Cell Biochem , vol.191 , pp. 187-199
    • McKendrick, L.1    Milne, D.2    Meek, D.3
  • 18
  • 19
    • 0030965244 scopus 로고    scopus 로고
    • Regulation of the DNA binding of p53 by its interaction with protein kinase CK2
    • Prowald A., Schuster N., Montenarh M. Regulation of the DNA binding of p53 by its interaction with protein kinase CK2. FEBS Lett 1997, 408:99-104.
    • (1997) FEBS Lett , vol.408 , pp. 99-104
    • Prowald, A.1    Schuster, N.2    Montenarh, M.3
  • 20
    • 33646140913 scopus 로고    scopus 로고
    • P53 stabilization and transactivation by a von Hippel-Lindau protein
    • Roe J.S., Kim H., Lee S.M., Kim S.T., Cho E.J., Youn H.D. p53 stabilization and transactivation by a von Hippel-Lindau protein. Mol Cell 2006, 22:395-405.
    • (2006) Mol Cell , vol.22 , pp. 395-405
    • Roe, J.S.1    Kim, H.2    Lee, S.M.3    Kim, S.T.4    Cho, E.J.5    Youn, H.D.6
  • 21
    • 33749663052 scopus 로고    scopus 로고
    • The positive regulation of p53 by the tumor suppressor VHL
    • Roe J.S., Youn H.D. The positive regulation of p53 by the tumor suppressor VHL. Cell Cycle 2006, 5:2054-2056.
    • (2006) Cell Cycle , vol.5 , pp. 2054-2056
    • Roe, J.S.1    Youn, H.D.2
  • 22
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2')
    • Sarno S., Reddy H., Meggio F., Ruzzene M., Davies S.P., Donella-Deana A., et al. Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2'). FEBS Lett 2001, 496:44-48.
    • (2001) FEBS Lett , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3    Ruzzene, M.4    Davies, S.P.5    Donella-Deana, A.6
  • 24
    • 70349186117 scopus 로고    scopus 로고
    • From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St-Denis N.A., Litchfield D.W. From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival. Cell Mol Life Sci 2009, 66:1817-1829.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 25
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • Stebbins C.E., Kaelin W.G., Pavletich N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 1999, 284:455-461.
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 26
    • 0035966127 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex
    • Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R. Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem 2001, 276:48627-48630.
    • (2001) J Biol Chem , vol.276 , pp. 48627-48630
    • Vazquez, F.1    Grossman, S.R.2    Takahashi, Y.3    Rokas, M.V.4    Nakamura, N.5    Sellers, W.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.