메뉴 건너뛰기




Volumn 13, Issue 3, 2014, Pages 780-791

F-box Protein FBXL16 Binds PP2A-B55αand Regulates Differentiation of Embryonic Stem Cells along the FLK1α Lineage

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2A; REPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE; VASCULOTROPIN RECEPTOR 2; VIMENTIN;

EID: 84895552992     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.031765     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 39349106325 scopus 로고    scopus 로고
    • Differentiation of embryonic stem cells to clinically relevant populations: Lessons from embryonic development
    • Murry, C. E., and Keller, G. (2008) Differentiation of embryonic stem cells to clinically relevant populations: lessons from embryonic development. Cell 132, 661-680
    • (2008) Cell , vol.132 , pp. 661-680
    • Murry, C.E.1    Keller, G.2
  • 2
    • 43749100265 scopus 로고    scopus 로고
    • Stem-cell-based therapy and lessons from the heart
    • Passier, R., van Laake, L. W., and Mummery, C. L. (2008) Stem-cell-based therapy and lessons from the heart. Nature 453, 322-329
    • (2008) Nature , vol.453 , pp. 322-329
    • Passier, R.1    Van Laake, L.W.2    Mummery, C.L.3
  • 3
    • 33748621746 scopus 로고    scopus 로고
    • Making or breaking the heart: From lineage determination to morphogenesis
    • Srivastava, D. (2006) Making or breaking the heart: from lineage determination to morphogenesis. Cell 126, 1037-1048
    • (2006) Cell , vol.126 , pp. 1037-1048
    • Srivastava, D.1
  • 6
    • 77955155919 scopus 로고    scopus 로고
    • The multiple phases and faces of wnt signaling during cardiac differentiation and development
    • Gessert, S., and Kuhl, M. (2010) The multiple phases and faces of wnt signaling during cardiac differentiation and development. Circ. Res. 107, 186-199
    • (2010) Circ. Res , vol.107 , pp. 186-199
    • Gessert, S.1    Kuhl, M.2
  • 7
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang, L. E., Gu, J., Schau, M., and Bunn, H. F. (1998) Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. U.S.A. 95, 7987-7992
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 8
    • 33646757232 scopus 로고    scopus 로고
    • The complexity of p53 stabilization and activation
    • Lavin, M. F., and Gueven, N. (2006) The complexity of p53 stabilization and activation. Cell Death Differ. 13, 941-950
    • (2006) Cell Death Differ , vol.13 , pp. 941-950
    • Lavin, M.F.1    Gueven, N.2
  • 9
    • 77957005350 scopus 로고    scopus 로고
    • The various roles of ubiquitin in Wnt pathway regulation
    • Tauriello, D. V., and Maurice, M. M. (2010) The various roles of ubiquitin in Wnt pathway regulation. Cell Cycle 9, 3700-3709
    • (2010) Cell Cycle , vol.9 , pp. 3700-3709
    • Tauriello, D.V.1    Maurice, M.M.2
  • 12
    • 67650088235 scopus 로고    scopus 로고
    • Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal development
    • Saiga, T., Fukuda, T., Matsumoto, M., Tada, H., Okano, H. J., Okano, H., and Nakayama, K. I. (2009) Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal development. Mol. Cell. Biol. 29,3529-3543
    • (2009) Mol. Cell. Biol , vol.29 , pp. 3529-3543
    • Saiga, T.1    Fukuda, T.2    Matsumoto, M.3    Tada, H.4    Okano, H.J.5    Okano, H.6    Nakayama, K.I.7
  • 13
    • 69849083542 scopus 로고    scopus 로고
    • The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73
    • Peschiaroli, A., Scialpi, F., Bernassola, F., Pagano, M., and Melino, G. (2009) The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73. Oncogene 28, 3157-3166
    • (2009) Oncogene , vol.28 , pp. 3157-3166
    • Peschiaroli, A.1    Scialpi, F.2    Bernassola, F.3    Pagano, M.4    Melino, G.5
  • 14
    • 79955757481 scopus 로고    scopus 로고
    • The steady-state repertoire of human SCF ubiquitin ligase complexes does not require ongoing Nedd8 conjugation
    • M110.006460
    • Lee, J. E., Sweredoski, M. J., Graham, R. L., Kolawa, N. J., Smith, G. T., Hess, S., and Deshaies, R. J. (2011) The steady-state repertoire of human SCF ubiquitin ligase complexes does not require ongoing Nedd8 conjugation. Mol. Cell. Proteomics 10, M110.006460
    • (2011) Mol. Cell. Proteomics , vol.10
    • Lee, J.E.1    Sweredoski, M.J.2    Graham, R.L.3    Kolawa, N.J.4    Smith, G.T.5    Hess, S.6    Deshaies, R.J.7
  • 15
    • 79960726254 scopus 로고    scopus 로고
    • Phosphatases: Providing safe passage through mitotic exit
    • Wurzenberger, C., and Gerlich, D. W. (2011) Phosphatases: providing safe passage through mitotic exit. Nat. Rev. Mol. Cell Biol. 12, 469-482
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 469-482
    • Wurzenberger, C.1    Gerlich, D.W.2
  • 16
    • 28244472754 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling regulates cardiogenesis of embryonic stem cells
    • Hakuno, D., Takahashi, T., Lammerding, J., and Lee, R. T. (2005) Focal adhesion kinase signaling regulates cardiogenesis of embryonic stem cells. J. Biol. Chem. 280, 39534-39544
    • (2005) J. Biol. Chem , vol.280 , pp. 39534-39544
    • Hakuno, D.1    Takahashi, T.2    Lammerding, J.3    Lee, R.T.4
  • 17
    • 30144432172 scopus 로고    scopus 로고
    • Deletion of the selection cassette, but not cis-acting elements, in targeted Flk1-lacZ allele reveals Flk1 expression in multipotent mesodermal progenitors
    • Ema, M., Takahashi, S., and Rossant, J. (2006) Deletion of the selection cassette, but not cis-acting elements, in targeted Flk1-lacZ allele reveals Flk1 expression in multipotent mesodermal progenitors. Blood 107, 111-117
    • (2006) Blood , vol.107 , pp. 111-117
    • Ema, M.1    Takahashi, S.2    Rossant, J.3
  • 18
    • 3543148255 scopus 로고    scopus 로고
    • N-terminal polyubiquitination and degradation of the Arf tumor suppressor
    • Kuo, M. L., den Besten, W., Bertwistle, D., Roussel, M. F., and Sherr, C. J. (2004) N-terminal polyubiquitination and degradation of the Arf tumor suppressor. Genes Dev. 18, 1862-1874
    • (2004) Genes Dev , vol.18 , pp. 1862-1874
    • Kuo, M.L.1    Den Besten, W.2    Bertwistle, D.3    Roussel, M.F.4    Sherr, C.J.5
  • 20
    • 79952306399 scopus 로고    scopus 로고
    • COMPASS: A suite of pre-and post-search proteomics software tools for OMSSA
    • Wenger, C. D., Phanstiel, D. H., Lee, M. V., Bailey, D. J., and Coon, J. J. (2011) COMPASS: a suite of pre-and post-search proteomics software tools for OMSSA. Proteomics 11, 1064-1074
    • (2011) Proteomics , vol.11 , pp. 1064-1074
    • Wenger, C.D.1    Phanstiel, D.H.2    Lee, M.V.3    Bailey, D.J.4    Coon, J.J.5
  • 22
  • 23
    • 76149132007 scopus 로고    scopus 로고
    • Comparison of database search strategies for high precursor mass accuracy MS/MS data
    • Hsieh, E. J., Hoopmann, M. R., MacLean, B., and MacCoss, M. J. (2010) Comparison of database search strategies for high precursor mass accuracy MS/MS data. J. Proteome Res. 9, 1138-1143
    • (2010) J. Proteome Res , vol.9 , pp. 1138-1143
    • Hsieh, E.J.1    Hoopmann, M.R.2    Maclean, B.3    Maccoss, M.J.4
  • 24
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • Nesvizhskii, A. I., and Aebersold, R. (2005) Interpretation of shotgun proteomic data: the protein inference problem. Mol. Cell. Proteomics 4, 1419-1440
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 26
    • 59049086847 scopus 로고    scopus 로고
    • Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
    • Swaney, D. L., Wenger, C. D., Thomson, J. A., and Coon, J. J. (2009) Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 106, 995-1000
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 995-1000
    • Swaney, D.L.1    Wenger, C.D.2    Thomson, J.A.3    Coon, J.J.4
  • 27
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha, A., and Deshaies, R. J. (2008) Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 32, 21-31
    • (2008) Mol. Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 28
    • 71449123070 scopus 로고    scopus 로고
    • Detection of sequential polyubiquitylation on a millisecond timescale
    • Pierce, N. W., Kleiger, G., Shan, S. O., and Deshaies, R. J. (2009) Detection of sequential polyubiquitylation on a millisecond timescale. Nature 462, 615-619
    • (2009) Nature , vol.462 , pp. 615-619
    • Pierce, N.W.1    Kleiger, G.2    Shan, S.O.3    Deshaies, R.J.4
  • 29
    • 33750456216 scopus 로고    scopus 로고
    • Multipotent flk-1+cardiovascular progenitor cells give rise to the cardiomyocyte, endothelial, and vascular smooth muscle lineages
    • Kattman, S. J., Huber, T. L., and Keller, G. M. (2006) Multipotent flk-1+cardiovascular progenitor cells give rise to the cardiomyocyte, endothelial, and vascular smooth muscle lineages. Dev. Cell 11, 723-732
    • (2006) Dev. Cell , vol.11 , pp. 723-732
    • Kattman, S.J.1    Huber, T.L.2    Keller, G.M.3
  • 30
    • 39149130361 scopus 로고    scopus 로고
    • Stem cells, the molecular circuitry of pluripotency and nuclear reprogramming
    • Jaenisch, R., and Young, R. (2008) Stem cells, the molecular circuitry of pluripotency and nuclear reprogramming. Cell 132, 567-582
    • (2008) Cell , vol.132 , pp. 567-582
    • Jaenisch, R.1    Young, R.2
  • 31
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics
    • Bennett, E. J., Rush, J., Gygi, S. P., and Harper, J. W. (2010) Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 143, 951-965
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1    Rush, J.2    Gygi, S.P.3    Harper, J.W.4
  • 32
    • 61649127812 scopus 로고    scopus 로고
    • From promiscuity to precision: Protein phosphatases get a makeover
    • Virshup, D. M., and Shenolikar, S. (2009) From promiscuity to precision: protein phosphatases get a makeover. Mol. Cell 33, 537-545
    • (2009) Mol. Cell , vol.33 , pp. 537-545
    • Virshup, D.M.1    Shenolikar, S.2
  • 35
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li, M., Makkinje, A., and Damuni, Z. (1996) The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 271, 11059-11062
    • (1996) J. Biol. Chem , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 36
    • 78650366525 scopus 로고    scopus 로고
    • Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis
    • Mochida, S., Maslen, S. L., Skehel, M., and Hunt, T. (2010) Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. Science 330, 1670-1673
    • (2010) Science , vol.330 , pp. 1670-1673
    • Mochida, S.1    Maslen, S.L.2    Skehel, M.3    Hunt, T.4
  • 37
    • 69249100506 scopus 로고    scopus 로고
    • PR55 alpha, a regulatory subunit of PP2A, specifically regulates PP2A-mediated beta-catenin dephosphorylation
    • Zhang, W., Yang, J., Liu, Y., Chen, X., Yu, T., Jia, J., and Liu, C. (2009) PR55 alpha, a regulatory subunit of PP2A, specifically regulates PP2A-mediated beta-catenin dephosphorylation. J. Biol. Chem. 284, 22649-22656
    • (2009) J. Biol. Chem , vol.284 , pp. 22649-22656
    • Zhang, W.1    Yang, J.2    Liu, Y.3    Chen, X.4    Yu, T.5    Jia, J.6    Liu, C.7
  • 38
    • 63649139204 scopus 로고    scopus 로고
    • Peptide quantification using 8-plex isobaric tags and electron transfer dissociation tandem mass spectrometry
    • Phanstiel, D., Unwin, R., McAlister, G. C., and Coon, J. J. (2009) Peptide quantification using 8-plex isobaric tags and electron transfer dissociation tandem mass spectrometry. Anal. Chem. 81, 1693-1698
    • (2009) Anal. Chem , vol.81 , pp. 1693-1698
    • Phanstiel, D.1    Unwin, R.2    McAlister, G.C.3    Coon, J.J.4
  • 39
    • 0032978487 scopus 로고    scopus 로고
    • Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55
    • Turowski, P., Myles, T., Hemmings, B. A., Fernandez, A., and Lamb, N. J. (1999) Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol. Biol. Cell 10, 1997-2015
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1997-2015
    • Turowski, P.1    Myles, T.2    Hemmings, B.A.3    Fernandez, A.4    Lamb, N.J.5
  • 41
    • 0030662073 scopus 로고    scopus 로고
    • Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation
    • Kaplan, K. B., Hyman, A. A., and Sorger, P. K. (1997) Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation. Cell 91, 491-500
    • (1997) Cell , vol.91 , pp. 491-500
    • Kaplan, K.B.1    Hyman, A.A.2    Sorger, P.K.3
  • 42
    • 69749123290 scopus 로고    scopus 로고
    • F-box-directed CRL complex assembly and regulation by the CSN and CAND1
    • Schmidt, M. W., McQuary, P. R., Wee, S., Hofmann, K., and Wolf, D. A. (2009) F-box-directed CRL complex assembly and regulation by the CSN and CAND1. Mol. Cell 35, 586-597
    • (2009) Mol. Cell , vol.35 , pp. 586-597
    • Schmidt, M.W.1    McQuary, P.R.2    Wee, S.3    Hofmann, K.4    Wolf, D.A.5
  • 43
    • 0034602831 scopus 로고    scopus 로고
    • The VacA toxin of Helicobacter pylori identifies a new intermediate filament-interacting protein
    • de Bernard, M., Moschioni, M., Napolitani, G., Rappuoli, R., and Montecucco, C. (2000) The VacA toxin of Helicobacter pylori identifies a new intermediate filament-interacting protein. EMBO J. 19, 48-56
    • (2000) EMBO J , vol.19 , pp. 48-56
    • De Bernard, M.1    Moschioni, M.2    Napolitani, G.3    Rappuoli, R.4    Montecucco, C.5
  • 44
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs, E., and Weber, K. (1994) Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63, 345-382
    • (1994) Annu. Rev. Biochem , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 45
    • 0024508983 scopus 로고
    • Changing patterns of cytokeratins and vimentin in the early chick embryo
    • Page, M. (1989) Changing patterns of cytokeratins and vimentin in the early chick embryo. Development 105, 97-107
    • (1989) Development , vol.105 , pp. 97-107
    • Page, M.1
  • 47
    • 0026016248 scopus 로고
    • Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: Inhibition by small-t antigen
    • Scheidtmann, K. H., Mumby, M. C., Rundell, K., and Walter, G. (1991) Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen. Mol. Cell. Biol. 11,1996-2003
    • (1991) Mol. Cell. Biol , vol.11 , pp. 1996-2003
    • Scheidtmann, K.H.1    Mumby, M.C.2    Rundell, K.3    Walter, G.4
  • 49
    • 41149175685 scopus 로고    scopus 로고
    • Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    • Xing, Y., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., and Shi, Y. (2008) Structural mechanism of demethylation and inactivation of protein phosphatase 2A. Cell 133, 154-163
    • (2008) Cell , vol.133 , pp. 154-163
    • Xing, Y.1    Li, Z.2    Chen, Y.3    Stock, J.B.4    Jeffrey, P.D.5    Shi, Y.6
  • 50
    • 43049112747 scopus 로고    scopus 로고
    • Protein phosphatase 2A (PP2A), a drugable tumor suppressor in Ph1(+) leukemias
    • Perrotti, D., and Neviani, P. (2008) Protein phosphatase 2A (PP2A), a drugable tumor suppressor in Ph1(+) leukemias. Cancer Metastasis Rev. 27, 159-168
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 159-168
    • Perrotti, D.1    Neviani, P.2
  • 51
    • 75449118483 scopus 로고    scopus 로고
    • FBXL16 is a novel E2F1-regulated gene commonly upregulated in p16INK4A-and p14ARFsilenced HeLa cells
    • Sato, K., Kusama, Y., Tategu, M., and Yoshida, K. (2010) FBXL16 is a novel E2F1-regulated gene commonly upregulated in p16INK4A-and p14ARFsilenced HeLa cells. Int. J. Oncol. 36, 479-490
    • (2010) Int. J. Oncol , vol.36 , pp. 479-490
    • Sato, K.1    Kusama, Y.2    Tategu, M.3    Yoshida, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.