메뉴 건너뛰기




Volumn 15, Issue 1, 2005, Pages 34-41

PP2A: The expected tumor suppressor

Author keywords

[No Author keywords available]

Indexed keywords

MYC PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2A; RAS PROTEIN; TELOMERASE; VIRUS LARGE T ANTIGEN;

EID: 12344308021     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2004.12.004     Document Type: Review
Times cited : (378)

References (55)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • D. Hanahan, and R.A. Weinberg The hallmarks of cancer Cell 100 2000 57 70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • V. Janssens, and J. Goris Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling Biochem J 353 2001 417 439
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 4
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • D.M. Virshup Protein phosphatase 2A: a panoply of enzymes Curr Opin Cell Biol 12 2000 180 185
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 5
    • 0035840446 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase 2A in cancer
    • A.H. Schönthal Role of serine/threonine protein phosphatase 2A in cancer Cancer Lett 170 2001 1 13
    • (2001) Cancer Lett , vol.170 , pp. 1-13
    • Schönthal, A.H.1
  • 6
    • 0037312507 scopus 로고    scopus 로고
    • Tor signalling in bugs, brain and brawn
    • E. Jacinto, and M.N. Hall Tor signalling in bugs, brain and brawn Nat Rev Mol Cell Biol 4 2003 117 126 Everything you need to know about Tor.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 7
    • 0037390203 scopus 로고    scopus 로고
    • The MID1/PP2A complex: A key to the pathogenesis of Opitz BBB/G syndrome
    • C catalysed by the ubiquitin-ligase activity of MID1 and requirement of α4 as the binding protein.
    • (2003) Bioessays , vol.25 , pp. 356-366
    • Schweiger, S.1    Schneider, R.2
  • 8
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • B. McCright, A.M. Rivers, S. Audlin, and D.M. Virshup The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation- induced phosphoproteins that target PP2A to both nucleus and cytoplasm J Biol Chem 271 1996 22081 22089
    • (1996) J Biol Chem , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 10
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • T.A. Millward, S. Zolnierowicz, and B.A. Hemmings Regulation of protein kinase cascades by protein phosphatase 2A Trends Biochem Sci 24 1999 186 191
    • (1999) Trends Biochem Sci , vol.24 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 11
    • 0034331359 scopus 로고    scopus 로고
    • Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
    • T. Tolstykh, J. Lee, S. Vafai, and J.B. Stock Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits EMBO J 19 2000 5682 5691
    • (2000) EMBO J , vol.19 , pp. 5682-5691
    • Tolstykh, T.1    Lee, J.2    Vafai, S.3    Stock, J.B.4
  • 12
    • 2642530239 scopus 로고    scopus 로고
    • An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator
    • S. Longin, J. Jordens, E. Martens, I. Stevens, V. Janssens, E. Rondelez, I. De Baere, R. Derua, E. Waelkens, J. Goris, and C. Van Hoof An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator Biochem J 380 2004 111 119 An inactive PP2A population was found associated with PME-1 throughout the purification process. This inactive form could be activated by PTPA, a protein that was previously identified by its potential to activate the phosphotyrosyl phosphatase activity of PP2A, and that is shown here to activate the Ser/Thr phosphatase activity of this 'special' inactive form of PP2A. If this mechanism can be proven in vivo, it might have far reaching consequences for our understanding of the regulation of PP2A.
    • (2004) Biochem J , vol.380 , pp. 111-119
    • Longin, S.1    Jordens, J.2    Martens, E.3    Stevens, I.4    Janssens, V.5    Rondelez, E.6    De Baere, I.7    Derua, R.8    Waelkens, E.9    Goris, J.10    Van Hoof, C.11
  • 13
    • 0041820233 scopus 로고    scopus 로고
    • A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo
    • T. Fellner, D.H. Lackner, H. Hombauer, P. Piribauer, I. Mudrak, K. Zaragoza, C. Juno, and E. Ogris A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo Genes Dev 17 2003 2138 2150
    • (2003) Genes Dev , vol.17 , pp. 2138-2150
    • Fellner, T.1    Lackner, D.H.2    Hombauer, H.3    Piribauer, P.4    Mudrak, I.5    Zaragoza, K.6    Juno, C.7    Ogris, E.8
  • 14
    • 0034622977 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue YPA1 of the mammalian phosphotyrosyl phosphatase activator of protein phosphatase 2A controls progression through the G1 phase of the yeast cell cycle
    • C. Van Hoof, V. Janssens, I. De Baere, H. de Winde, J. Winderickx, F. Dumortier, J. Thevelein, W. Merlevede, and J. Goris The Saccharomyces cerevisiae homologue YPA1 of the mammalian phosphotyrosyl phosphatase activator of protein phosphatase 2A controls progression through the G1 phase of the yeast cell cycle J Mol Biol 302 2000 103 119
    • (2000) J Mol Biol , vol.302 , pp. 103-119
    • Van Hoof, C.1    Janssens, V.2    De Baere, I.3    De Winde, H.4    Winderickx, J.5    Dumortier, F.6    Thevelein, J.7    Merlevede, W.8    Goris, J.9
  • 15
    • 0037085451 scopus 로고    scopus 로고
    • ATM-dependent dissociation of B55 regulatory subunit from nuclear PP2A in response to ionizing radiation
    • C.Y. Guo, D.L. Brautigan, and J.M. Larner ATM-dependent dissociation of B55 regulatory subunit from nuclear PP2A in response to ionizing radiation J Biol Chem 277 2002 4839 4844
    • (2002) J Biol Chem , vol.277 , pp. 4839-4844
    • Guo, C.Y.1    Brautigan, D.L.2    Larner, J.M.3
  • 16
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Y. Shiloh ATM and related protein kinases: safeguarding genome integrity Nat Rev Cancer 3 2003 155 168
    • (2003) Nat Rev Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 18
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases
    • C. Bialojan, and A. Takai Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases Biochem J 256 1988 283 290
    • (1988) Biochem J , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 19
    • 0025103372 scopus 로고
    • Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A
    • D.C. Pallas, L.K. Shahrik, B.L. Martin, T.B. Jaspers, T.B. Miller, D.L. Brautigan, and T.M. Roberts Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A Cell 60 1990 167 176
    • (1990) Cell , vol.60 , pp. 167-176
    • Pallas, D.C.1    Shahrik, L.K.2    Martin, B.L.3    Jaspers, T.B.4    Miller, T.B.5    Brautigan, D.L.6    Roberts, T.M.7
  • 21
    • 0029153084 scopus 로고
    • Deregulation of translational control of the 65-kDa regulatory subunit (PR65 alpha) of protein phosphatase 2A leads to multinucleated cells
    • S. Wera, A. Fernandez, N.J. Lamb, P. Turowski, M. Hemmings-Mieszczak, R.E. Mayer-Jaekel, and B.A. Hemmings Deregulation of translational control of the 65-kDa regulatory subunit (PR65 alpha) of protein phosphatase 2A leads to multinucleated cells J Biol Chem 270 1995 21374 21381
    • (1995) J Biol Chem , vol.270 , pp. 21374-21381
    • Wera, S.1    Fernandez, A.2    Lamb, N.J.3    Turowski, P.4    Hemmings-Mieszczak, M.5    Mayer-Jaekel, R.E.6    Hemmings, B.A.7
  • 22
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • M. Li, H. Guo, and Z. Damuni Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney Biochemistry 34 1995 1988 1996
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 23
    • 0030065261 scopus 로고    scopus 로고
    • Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila
    • D.A. Wassarman, N.M. Solomon, H.C. Chang, F.D. Karim, M. Therrien, and G.M. Rubin Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila Genes Dev 10 1996 272 278
    • (1996) Genes Dev , vol.10 , pp. 272-278
    • Wassarman, D.A.1    Solomon, N.M.2    Chang, H.C.3    Karim, F.D.4    Therrien, M.5    Rubin, G.M.6
  • 25
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • M.R. Groves, N. Hanlon, P. Turowski, B.A. Hemmings, and D. Barford The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs Cell 96 1999 99 110
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 26
    • 0033609688 scopus 로고    scopus 로고
    • Identification by differential display of a protein phosphatase-2A regulatory subunit preferentially expressed in malignant melanoma cells
    • G. Francia, R. Poulsom, A.M. Hanby, S.D. Mitchell, G. Williams, P. McKee, and I.R. Hart Identification by differential display of a protein phosphatase-2A regulatory subunit preferentially expressed in malignant melanoma cells Int J Cancer 82 1999 709 713
    • (1999) Int J Cancer , vol.82 , pp. 709-713
    • Francia, G.1    Poulsom, R.2    Hanby, A.M.3    Mitchell, S.D.4    Williams, G.5    McKee, P.6    Hart, I.R.7
  • 27
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A
    • J.M. Seeling, J.R. Miller, R. Gil, R.T. Moon, R. White, and D.M. Virshup Regulation of β-catenin signaling by the B56 subunit of protein phosphatase 2A Science 283 1999 2089 2091
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 28
    • 0034651747 scopus 로고    scopus 로고
    • A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
    • A. Ito, T.R. Kataoka, M. Watanabe, K. Nishiyama, Y. Mazaki, H. Sabe, Y. Kitamara, and H. Nojima A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation EMBO J 19 2000 562 571
    • (2000) EMBO J , vol.19 , pp. 562-571
    • Ito, A.1    Kataoka, T.R.2    Watanabe, M.3    Nishiyama, K.4    Mazaki, Y.5    Sabe, H.6    Kitamara, Y.7    Nojima, H.8
  • 29
    • 1442310493 scopus 로고    scopus 로고
    • Identification of specific PP2A complexes involved in human cell transformation
    • W. Chen, R. Possemato, K.T. Campbell, C.A. Plattner, D.C. Pallas, and W.C. Hahn Identification of specific PP2A complexes involved in human cell transformation Cancer Cell 5 2004 127 136 Following up their previous work [48], the authors tried to find conditions in which ST can be replaced in the experimental model to transform human cell lines with a minimal combination of genes. They found that the effects of suppression of PR61γ/B′ were very similar to the effects of ST in this model. This was unexpected because it was previously thought that ST was only able to expel PR55/B, and not PR61/B′, from their trimeric holoenzyme forms.
    • (2004) Cancer Cell , vol.5 , pp. 127-136
    • Chen, W.1    Possemato, R.2    Campbell, K.T.3    Plattner, C.A.4    Pallas, D.C.5    Hahn, W.C.6
  • 31
    • 0033916381 scopus 로고    scopus 로고
    • Alterations of the PPP2R1B gene located at 11q23 in human colorectal cancers
    • Y. Takagi, M. Futamura, K. Yamaguchi, S. Aoki, T. Takahashi, and S. Saji Alterations of the PPP2R1B gene located at 11q23 in human colorectal cancers Gut 47 2000 268 271
    • (2000) Gut , vol.47 , pp. 268-271
    • Takagi, Y.1    Futamura, M.2    Yamaguchi, K.3    Aoki, S.4    Takahashi, T.5    Saji, S.6
  • 32
    • 0034708257 scopus 로고    scopus 로고
    • Low frequency of alterations of the alpha (PPP2R1A) and beta (PPP2R1B) isoforms of the subunit a of the serine-threonine phosphatase 2A in human neoplasms
    • G.A. Calin, M.G. di Iasio, E. Caprini, I. Vorechovsky, P.G. Natali, G. Sozzi, C.M. Croce, G. Barnanti-Brodano, G. Russo, and M. Negrini Low frequency of alterations of the alpha (PPP2R1A) and beta (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2A in human neoplasms Oncogene 19 2000 1191 1195
    • (2000) Oncogene , vol.19 , pp. 1191-1195
    • Calin, G.A.1    Di Iasio, M.G.2    Caprini, E.3    Vorechovsky, I.4    Natali, P.G.5    Sozzi, G.6    Croce, C.M.7    Barnanti-Brodano, G.8    Russo, G.9    Negrini, M.10
  • 33
    • 0035804217 scopus 로고    scopus 로고
    • Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the a alpha subunit gene
    • R. Ruediger, H.T. Pham, and G. Walter Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene Oncogene 20 2001 10 15
    • (2001) Oncogene , vol.20 , pp. 10-15
    • Ruediger, R.1    Pham, H.T.2    Walter, G.3
  • 34
    • 0035883164 scopus 로고    scopus 로고
    • Reduced expression of the Aα subunit of protein phosphatase 2A in human gliomas in the absence of mutations in the Aα and Aβ subunit genes
    • S. Collela, H. Ohgaki, R. Ruediger, F. Yang, M. NakaRmura, H. Fujisawa, P. Kleihues, and G. Walter Reduced expression of the Aα subunit of protein phosphatase 2A in human gliomas in the absence of mutations in the Aα and Aβ subunit genes Int J Cancer 93 2001 798 804
    • (2001) Int J Cancer , vol.93 , pp. 798-804
    • Collela, S.1    Ohgaki, H.2    Ruediger, R.3    Yang, F.4    Nakarmura, M.5    Fujisawa, H.6    Kleihues, P.7    Walter, G.8
  • 35
    • 3142688531 scopus 로고    scopus 로고
    • Reduced expression of the regulatory a subunit of serine/threonine protein phosphatase 2A in human breast cancer MCF-7 cells
    • K. Suzuki, and K. Takahashi Reduced expression of the regulatory A subunit of serine/threonine protein phosphatase 2A in human breast cancer MCF-7 cells Int J Oncol 23 2003 1263 1268
    • (2003) Int J Oncol , vol.23 , pp. 1263-1268
    • Suzuki, K.1    Takahashi, K.2
  • 36
    • 0036096778 scopus 로고    scopus 로고
    • B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster
    • X. Li, A. Scuderi, A. Letsou, and D.M. Virshup B56-associated protein phosphatase 2A is required for survival and protects from apoptosis in Drosophila melanogaster Mol Cell Biol 22 2002 3674 3684
    • (2002) Mol Cell Biol , vol.22 , pp. 3674-3684
    • Li, X.1    Scuderi, A.2    Letsou, A.3    Virshup, D.M.4
  • 37
    • 0037007096 scopus 로고    scopus 로고
    • Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits
    • A.M. Silverstein, C.A. Barrow, A.J. Davis, and M.C. Mumby Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits Proc Natl Acad Sci USA 99 2002 4221 4226
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4221-4226
    • Silverstein, A.M.1    Barrow, C.A.2    Davis, A.J.3    Mumby, M.C.4
  • 38
    • 0037221975 scopus 로고    scopus 로고
    • A truncated isoform of the protein phosphatase 2A B56γ regulatory subunit may promote genetic instability and cause tumor progression
    • A. Ito, Y. Koma, K. Watabe, T. Nagano, Y. Endo, H. Nojima, and Y. Kitamara A truncated isoform of the protein phosphatase 2A B56γ regulatory subunit may promote genetic instability and cause tumor progression Am J Pathol 162 2003 81 91
    • (2003) Am J Pathol , vol.162 , pp. 81-91
    • Ito, A.1    Koma, Y.2    Watabe, K.3    Nagano, T.4    Endo, Y.5    Nojima, H.6    Kitamara, Y.7
  • 40
    • 1842559439 scopus 로고    scopus 로고
    • A truncated isoform of the PP2A B56gamma regulatory subunit reduces irradiation-induced Mdm2 phosphorylation and could contribute to metastatic melanoma cell radioresistance
    • Y.I. Koma, A. Ito, K. Watabe, S.H. Kimura, and Y. Kitamura A truncated isoform of the PP2A B56gamma regulatory subunit reduces irradiation-induced Mdm2 phosphorylation and could contribute to metastatic melanoma cell radioresistance Histol Histopathol 19 2004 391 400
    • (2004) Histol Histopathol , vol.19 , pp. 391-400
    • Koma, Y.I.1    Ito, A.2    Watabe, K.3    Kimura, S.H.4    Kitamura, Y.5
  • 41
    • 0029827632 scopus 로고    scopus 로고
    • P53-dependent association between cyclin G and the B′ subunit of protein phosphatase 2A
    • K. Okamoto, C. Kamibayashi, M. Serrano, C. Prives, M.C. Mumby, and D. Beach p53-dependent association between cyclin G and the B′ subunit of protein phosphatase 2A Mol Cell Biol 16 1996 6593 6602
    • (1996) Mol Cell Biol , vol.16 , pp. 6593-6602
    • Okamoto, K.1    Kamibayashi, C.2    Serrano, M.3    Prives, C.4    Mumby, M.C.5    Beach, D.6
  • 42
    • 0037178863 scopus 로고    scopus 로고
    • Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B′ subunits in active complexes and induces nuclear aberrations and G1/S phase cell cycle arrest
    • D.A. Bennin, A.S. Arachchige Don, T. Brake, J.L. McKenzie, H. Rosenbaum, L. Ortiz, A.A. DePaoli-Roach, and M.C. Horne Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B′ subunits in active complexes and induces nuclear aberrations and G1/S phase cell cycle arrest J Biol Chem 277 2002 27449 27467
    • (2002) J Biol Chem , vol.277 , pp. 27449-27467
    • Bennin, D.A.1    Arachchige Don, A.S.2    Brake, T.3    McKenzie, J.L.4    Rosenbaum, H.5    Ortiz, L.6    Depaoli-Roach, A.A.7    Horne, M.C.8
  • 43
    • 0036668475 scopus 로고    scopus 로고
    • Cyclin G1 associates with MDM2 and regulates accumulation and degradation of p53 protein
    • S.H. Kimura, and H. Nojima Cyclin G1 associates with MDM2 and regulates accumulation and degradation of p53 protein Genes Cells 7 2002 869 880
    • (2002) Genes Cells , vol.7 , pp. 869-880
    • Kimura, S.H.1    Nojima, H.2
  • 45
    • 0038702246 scopus 로고    scopus 로고
    • Phosphatases in apoptosis: To be or not to be, PP2A is in the heart of the question
    • C. Van Hoof, and J. Goris Phosphatases in apoptosis: to be or not to be, PP2A is in the heart of the question Biochim Biophys Acta 1640 2003 97 104
    • (2003) Biochim Biophys Acta , vol.1640 , pp. 97-104
    • Van Hoof, C.1    Goris, J.2
  • 46
    • 1342288971 scopus 로고    scopus 로고
    • Comparative biology of mouse versus human cells: Modeling human cancer in mice
    • A. Rangarajan, and R.A. Weinberg Comparative biology of mouse versus human cells: modeling human cancer in mice Nat Rev Cancer 3 2003 952 959
    • (2003) Nat Rev Cancer , vol.3 , pp. 952-959
    • Rangarajan, A.1    Weinberg, R.A.2
  • 47
    • 3042710564 scopus 로고    scopus 로고
    • Functional genetics and experimental models of human cancer
    • J.J. Zhao, T.M. Roberts, and W.C. Hahn Functional genetics and experimental models of human cancer Trends Mol Med 10 2004 344 350
    • (2004) Trends Mol Med , vol.10 , pp. 344-350
    • Zhao, J.J.1    Roberts, T.M.2    Hahn, W.C.3
  • 49
    • 1442285922 scopus 로고    scopus 로고
    • PP2A fulfills its promises as tumor suppressor: Which subunits are important?
    • C. Van Hoof, and J. Goris PP2A fulfills its promises as tumor suppressor: which subunits are important? Cancer Cell 5 2004 105 106
    • (2004) Cancer Cell , vol.5 , pp. 105-106
    • Van Hoof, C.1    Goris, J.2
  • 50
    • 0034306997 scopus 로고    scopus 로고
    • Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability
    • R. Sears, F. Nuckolls, E. Haura, Y. Taya, K. Tamai, and J.R. Nevins Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability Genes Dev 14 2000 2501 2514
    • (2000) Genes Dev , vol.14 , pp. 2501-2514
    • Sears, R.1    Nuckolls, F.2    Haura, E.3    Taya, Y.4    Tamai, K.5    Nevins, J.R.6
  • 51
    • 0042972556 scopus 로고    scopus 로고
    • Ras modulates Myc activity to repress thrombospondin-1 expression and increase tumor angiogenesis
    • R.S. Watnick, Y.-N. Cheng, A. Rangarajan, T.A. Ince, and R.A. Weinberg Ras modulates Myc activity to repress thrombospondin-1 expression and increase tumor angiogenesis Cancer Cell 3 2003 219 231 Tumor vascularisation is essential for growth of tumors beyond 1-2 mm in diameter. The authors dissect how a well-equilibrated balance of anti-angiogenic (trombospondin-1) and pro-angiogenic (VEGF) factors is obtained by a novel described effector-pathway of Ras that leads to activation of Myc through phosphorylation (PI3K, Rho, ROCK) and repression of trombospondin-1.
    • (2003) Cancer Cell , vol.3 , pp. 219-231
    • Watnick, R.S.1    Cheng, Y.-N.2    Rangarajan, A.3    Ince, T.A.4    Weinberg, R.A.5
  • 52
    • 0036781812 scopus 로고    scopus 로고
    • C-Myc: More than just a matter of life and death
    • S. Pelengaris, M. Khan, and G. Evan c-Myc: more than just a matter of life and death Nat Rev Cancer 2 2002 764 776
    • (2002) Nat Rev Cancer , vol.2 , pp. 764-776
    • Pelengaris, S.1    Khan, M.2    Evan, G.3
  • 53
    • 0344784889 scopus 로고    scopus 로고
    • Human mammary epithelial cell transformation through the activation of phosphatidylinositol 3-kinase
    • J.J. Zhao, O.V. Gjoerup, R.R. Subramanian, Y. Cheng, W. Chen, T.M. Roberts, and W.C. Hahn Human mammary epithelial cell transformation through the activation of phosphatidylinositol 3-kinase Cancer Cell 3 2003 483 495 ST activates the PI3K pathway, and constitutively active PI3K signaling can substitute for ST in transformation. Using constitutively active versions of Akt1 and Rac1, it is shown that these downstream pathways of PI3K synergize to achieve anchorage-independent growth. At lower levels of c-myc expression, activated PI3K also replaces ST in anchorage independent growth and tumorigenicity of cells containing oncogenic ras and LT. However, elevated c-myc expression could not replace oncogenic ras for tumorigenesis.
    • (2003) Cancer Cell , vol.3 , pp. 483-495
    • Zhao, J.J.1    Gjoerup, O.V.2    Subramanian, R.R.3    Cheng, Y.4    Chen, W.5    Roberts, T.M.6    Hahn, W.C.7
  • 54
    • 0037370611 scopus 로고    scopus 로고
    • Simian virus 40 small tumor antigen induces deregulation of the actin cytoskeleton and tight junctions in kidney epithelial cells
    • V. Nunbhakdi-Craig, L. Craig, T. Machleidt, and E. Sontag Simian virus 40 small tumor antigen induces deregulation of the actin cytoskeleton and tight junctions in kidney epithelial cells J Virol 77 2003 2807 2818
    • (2003) J Virol , vol.77 , pp. 2807-2818
    • Nunbhakdi-Craig, V.1    Craig, L.2    MacHleidt, T.3    Sontag, E.4
  • 55
    • 5044220058 scopus 로고    scopus 로고
    • Signaling and transcriptional changes critical for transformation of human cells by Simian virus 40 small tumor antigen or protein phosphatase 2A B56• knockdown
    • C.S. Moreno, S. Ramachandran, D.G. Ashby, N. Laycock, C.A. Plattner, W. Chen, W.C. Hahn, and D.C. Pallas Signaling and transcriptional changes critical for transformation of human cells by Simian virus 40 small tumor antigen or protein phosphatase 2A B56• knockdown Cancer Res 64 2004 6978 6988 See Update.
    • (2004) Cancer Res , vol.64 , pp. 6978-6988
    • Moreno, C.S.1    Ramachandran, S.2    Ashby, D.G.3    Laycock, N.4    Plattner, C.A.5    Chen, W.6    Hahn, W.C.7    Pallas, D.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.