메뉴 건너뛰기




Volumn 13, Issue 12, 2014, Pages 5860-5868

Kinetic analysis of BCL11B multisite phosphorylation-dephosphorylation and coupled sumoylation in primary thymocytes by multiple reaction monitoring mass spectroscopy

Author keywords

BCL11B; MRM; post translational modification; signal transduction; SRM; sumoylation; T cell receptor

Indexed keywords

LYSINE; MITOGEN ACTIVATED PROTEIN KINASE; PROLINE; SERINE; T LYMPHOCYTE RECEPTOR; THREONINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BCL11B; UNCLASSIFIED DRUG; BCL11B PROTEIN, MOUSE; CALCIMYCIN; CALCIUM IONOPHORE; PHORBOL DIBUTYRATE; REPRESSOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84915745293     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr5007697     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 84895077483 scopus 로고    scopus 로고
    • Regulation of Transcription Factor Activity by Interconnected Post-Translational Modifications
    • Filtz, T. M.; Vogel, W. K.; Leid, M. Regulation of Transcription Factor Activity by Interconnected Post-Translational Modifications Trends Pharmacol. Sci. 2014, 35, 76-85
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 76-85
    • Filtz, T.M.1    Vogel, W.K.2    Leid, M.3
  • 2
    • 79961091829 scopus 로고    scopus 로고
    • Serine 105 Phosphorylation of Transcription Factor GATA4 is Necessary for Stress-Induced Cardiac Hypertrophy in Vivo
    • van Berlo, J. H.; Elrod, J. W.; Aronow, B. J.; Pu, W. T.; Molkentin, J. D. Serine 105 Phosphorylation of Transcription Factor GATA4 Is Necessary for Stress-Induced Cardiac Hypertrophy in Vivo Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 12331-12336
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12331-12336
    • Van Berlo, J.H.1    Elrod, J.W.2    Aronow, B.J.3    Pu, W.T.4    Molkentin, J.D.5
  • 3
    • 43049121301 scopus 로고    scopus 로고
    • A Tumor Suppressor Role for PP2A-B56α through Negative Regulation of c-Myc and Other Key Oncoproteins
    • Arnold, H. K.; Sears, R. C. A Tumor Suppressor Role for PP2A-B56α through Negative Regulation of c-Myc and Other Key Oncoproteins Cancer Metastasis Rev. 2008, 27, 147-158
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 147-158
    • Arnold, H.K.1    Sears, R.C.2
  • 4
    • 84893781709 scopus 로고    scopus 로고
    • Protein Post-Translational Modifications and Regulation of Pluripotency in Human Stem Cells
    • Wang, Y.-C.; Peterson, S. E.; Loring, J. F. Protein Post-Translational Modifications and Regulation of Pluripotency in Human Stem Cells Cell Res. 2014, 24, 143-160
    • (2014) Cell Res. , vol.24 , pp. 143-160
    • Wang, Y.-C.1    Peterson, S.E.2    Loring, J.F.3
  • 7
    • 84861308595 scopus 로고    scopus 로고
    • BCL11B Regulates Epithelial Proliferation and Asymmetric Development of the Mouse Mandibular Incisor
    • Kyrylkova, K.; Kyryachenko, S.; Biehs, B.; Klein, O.; Kioussi, C.; Leid, M. BCL11B Regulates Epithelial Proliferation and Asymmetric Development of the Mouse Mandibular Incisor PLoS One 2012, 7, e37670
    • (2012) PLoS One , vol.7 , pp. 37670
    • Kyrylkova, K.1    Kyryachenko, S.2    Biehs, B.3    Klein, O.4    Kioussi, C.5    Leid, M.6
  • 8
    • 38349029763 scopus 로고    scopus 로고
    • Ctip2 Controls the Differentiation of Medium Spiny Neurons and the Establishment of the Cellular Architecture of the Striatum
    • Arlotta, P.; Molyneaux, B. J.; Jabaudon, D.; Yoshida, Y.; Macklis, J. D. Ctip2 Controls the Differentiation of Medium Spiny Neurons and the Establishment of the Cellular Architecture of the Striatum J. Neurosci. 2008, 28, 622-632
    • (2008) J. Neurosci. , vol.28 , pp. 622-632
    • Arlotta, P.1    Molyneaux, B.J.2    Jabaudon, D.3    Yoshida, Y.4    MacKlis, J.D.5
  • 12
    • 77954329976 scopus 로고    scopus 로고
    • An Early T-Cell Lineage Commitment Checkpoint Dependent on the Transcription Factor Bcl11b
    • Li, L.; Leid, M.; Rothenberg, E. V. An Early T-Cell Lineage Commitment Checkpoint Dependent on the Transcription Factor Bcl11b Science 2010, 329, 89-93
    • (2010) Science , vol.329 , pp. 89-93
    • Li, L.1    Leid, M.2    Rothenberg, E.V.3
  • 17
    • 0141613827 scopus 로고    scopus 로고
    • T(5;14)/HOX11L2-Positive T-Cell Acute Lymphoblastic Leukemia. A Collaborative Study of the Groupe Français de Cytogénétique Hématologique (GFCH)
    • Berger, R.; Dastugue, N.; Busson, M.; Van Den Akker, J.; Pérot, C.; Ballerini, P.; Hagemeijer, A.; Michaux, L.; Charrin, C.; Pages, M. P. t(5;14)/HOX11L2-Positive T-Cell Acute Lymphoblastic Leukemia. A Collaborative Study of the Groupe Français de Cytogénétique Hématologique (GFCH) Leukemia 2003, 17, 1851-1857
    • (2003) Leukemia , vol.17 , pp. 1851-1857
    • Berger, R.1    Dastugue, N.2    Busson, M.3    Van Den Akker, J.4    Pérot, C.5    Ballerini, P.6    Hagemeijer, A.7    Michaux, L.8    Charrin, C.9    Pages, M.P.10
  • 18
    • 0037403157 scopus 로고    scopus 로고
    • Activation of HOX11L2 by Juxtaposition with 3′- BCL11B in an Acute Lymphoblastic Leukemia Cell Line (HPB-ALL) with t(5;14)(q35;q32.2)
    • MacLeod, R. A. F.; Nagel, S.; Kaufmann, M.; Janssen, J. W. G.; Drexler, H. G. Activation of HOX11L2 by Juxtaposition with 3′- BCL11B in an Acute Lymphoblastic Leukemia Cell Line (HPB-ALL) with t(5;14)(q35;q32.2) Genes, Chromosomes Cancer 2003, 37, 84-91
    • (2003) Genes, Chromosomes Cancer , vol.37 , pp. 84-91
    • MacLeod, R.A.F.1    Nagel, S.2    Kaufmann, M.3    Janssen, J.W.G.4    Drexler, H.G.5
  • 19
    • 84873838326 scopus 로고    scopus 로고
    • Reduced Level of the BCL11B Protein is Associated with Adult T-Cell Leukemia/Lymphoma
    • Kurosawa, N.; Fujimoto, R.; Ozawa, T.; Itoyama, T.; Sadamori, N.; Isobe, M. Reduced Level of the BCL11B Protein Is Associated with Adult T-Cell Leukemia/Lymphoma PLoS One 2013, 8, e55147
    • (2013) PLoS One , vol.8 , pp. 55147
    • Kurosawa, N.1    Fujimoto, R.2    Ozawa, T.3    Itoyama, T.4    Sadamori, N.5    Isobe, M.6
  • 23
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A Comprehensive Resource for Investigating the Structure and Function of Experimentally Determined Post-Translational Modifications in Man and Mouse
    • Hornbeck, P. V.; Kornhauser, J. M.; Tkachev, S.; Zhang, B.; Skrzypek, E.; Murray, B.; Latham, V.; Sullivan, M. PhosphoSitePlus: A Comprehensive Resource for Investigating the Structure and Function of Experimentally Determined Post-Translational Modifications in Man and Mouse Nucleic Acids Res. 2012, 40, D261-D270
    • (2012) Nucleic Acids Res. , vol.40 , pp. 261-D270
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 24
    • 84864533993 scopus 로고    scopus 로고
    • Coordinated Regulation of Transcription Factor Bcl11b Activity in Thymocytes by the Mitogen-Activated Protein Kinase (MAPK) Pathways and Protein Sumoylation
    • Zhang, L.-J.; Vogel, W. K.; Liu, X.; Topark-Ngarm, A.; Arbogast, B. L.; Maier, C. S.; Filtz, T. M.; Leid, M. Coordinated Regulation of Transcription Factor Bcl11b Activity in Thymocytes by the Mitogen-Activated Protein Kinase (MAPK) Pathways and Protein Sumoylation J. Biol. Chem. 2012, 287, 26971-26988
    • (2012) J. Biol. Chem. , vol.287 , pp. 26971-26988
    • Zhang, L.-J.1    Vogel, W.K.2    Liu, X.3    Topark-Ngarm, A.4    Arbogast, B.L.5    Maier, C.S.6    Filtz, T.M.7    Leid, M.8
  • 26
    • 0030586654 scopus 로고    scopus 로고
    • Phorbol Ester and Calcium Ionophore Can Replace TCR Signals That Induce Positive Selection of CD4 T-Cells
    • Takahama, Y.; Nakauchi, H. Phorbol Ester and Calcium Ionophore Can Replace TCR Signals That Induce Positive Selection of CD4 T-Cells J. Immunol. 1996, 157, 1508-1513
    • (1996) J. Immunol. , vol.157 , pp. 1508-1513
    • Takahama, Y.1    Nakauchi, H.2
  • 27
    • 33747626954 scopus 로고    scopus 로고
    • Analysis of Peptide MS/MS Spectra from Large-Scale Proteomics Experiments Using Spectrum Libraries
    • Frewen, B. E.; Merrihew, G. E.; Wu, C. C.; Noble, W. S.; MacCoss, M. J. Analysis of Peptide MS/MS Spectra from Large-Scale Proteomics Experiments Using Spectrum Libraries Anal. Chem. 2006, 78, 5678-5684
    • (2006) Anal. Chem. , vol.78 , pp. 5678-5684
    • Frewen, B.E.1    Merrihew, G.E.2    Wu, C.C.3    Noble, W.S.4    MacCoss, M.J.5
  • 28
    • 78650355102 scopus 로고    scopus 로고
    • Effect of Collision Energy Optimization on the Measurement of Peptides by Selected Reaction Monitoring (SRM) Mass Spectrometry
    • Maclean, B.; Tomazela, D. M.; Abbatiello, S. E.; Zhang, S.; Whiteaker, J. R.; Paulovich, A. G.; Carr, S. A.; MacCoss, M. J. Effect of Collision Energy Optimization on the Measurement of Peptides by Selected Reaction Monitoring (SRM) Mass Spectrometry Anal. Chem. 2010, 82, 10116-10124
    • (2010) Anal. Chem. , vol.82 , pp. 10116-10124
    • MacLean, B.1    Tomazela, D.M.2    Abbatiello, S.E.3    Zhang, S.4    Whiteaker, J.R.5    Paulovich, A.G.6    Carr, S.A.7    MacCoss, M.J.8
  • 30
    • 73049160443 scopus 로고
    • Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic Ribonuclease
    • Gross, E.; Witkop, B. Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic Ribonuclease J. Biol. Chem. 1962, 237, 1856-1860
    • (1962) J. Biol. Chem. , vol.237 , pp. 1856-1860
    • Gross, E.1    Witkop, B.2
  • 32
    • 84883175765 scopus 로고    scopus 로고
    • Multisite Light-Induced Phosphorylation of the Transcription Factor PIF3 is Necessary for Both Its Rapid Degradation and Concomitant Negative Feedback Modulation of Photoreceptor phyB Levels in Arabidopsis
    • Ni, W.; Xu, S.-L.; Chalkley, R. J.; Pham, T. N. D.; Guan, S.; Maltby, D. A.; Burlingame, A. L.; Wang, Z.-Y.; Quail, P. H. Multisite Light-Induced Phosphorylation of the Transcription Factor PIF3 Is Necessary for Both Its Rapid Degradation and Concomitant Negative Feedback Modulation of Photoreceptor phyB Levels in Arabidopsis Plant Cell 2013, 25, 2679-2698
    • (2013) Plant Cell , vol.25 , pp. 2679-2698
    • Ni, W.1    Xu, S.-L.2    Chalkley, R.J.3    Pham, T.N.D.4    Guan, S.5    Maltby, D.A.6    Burlingame, A.L.7    Wang, Z.-Y.8    Quail, P.H.9
  • 33
    • 84878860782 scopus 로고    scopus 로고
    • A Posttranslational Modification Cascade Involving p38, Tip60, and PRAK Mediates Oncogene-Induced Senescence
    • Zheng, H.; Seit-Nebi, A.; Han, X.; Aslanian, A.; Tat, J.; Liao, R.; Yates, J. R.; Sun, P. A Posttranslational Modification Cascade Involving p38, Tip60, and PRAK Mediates Oncogene-Induced Senescence Mol. Cell 2013, 50, 699-710
    • (2013) Mol. Cell , vol.50 , pp. 699-710
    • Zheng, H.1    Seit-Nebi, A.2    Han, X.3    Aslanian, A.4    Tat, J.5    Liao, R.6    Yates, J.R.7    Sun, P.8
  • 34
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative Phosphoproteomic Analysis of T-Cell Receptor Signaling Reveals System-Wide Modulation of Protein-Protein Interactions
    • Mayya, V.; Lundgren, D. H.; Hwang, S.-I.; Rezaul, K.; Wu, L.; Eng, J. K.; Rodionov, V.; Han, D. K. Quantitative Phosphoproteomic Analysis of T-Cell Receptor Signaling Reveals System-Wide Modulation of Protein-Protein Interactions Sci. Signal. 2009, 2, ra46
    • (2009) Sci. Signal. , vol.2 , pp. 46
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.-I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 36
    • 13444260275 scopus 로고    scopus 로고
    • The Absolute Quantification Strategy: A General Procedure for the Quantification of Proteins and Post-Translational Modifications
    • Kirkpatrick, D. S.; Gerber, S. A.; Gygi, S. P. The Absolute Quantification Strategy: A General Procedure for the Quantification of Proteins and Post-Translational Modifications Methods 2005, 35, 265-273
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 37
    • 55249096736 scopus 로고    scopus 로고
    • The Fast-Growing Business of SUMO Chains
    • Ulrich, H. D. The Fast-Growing Business of SUMO Chains Mol. Cell 2008, 32, 301-305
    • (2008) Mol. Cell , vol.32 , pp. 301-305
    • Ulrich, H.D.1
  • 38
    • 0037405246 scopus 로고    scopus 로고
    • Recruitment of Tat to Heterochromatin Protein HP1 via Interaction with CTIP2 Inhibits Human Immunodeficiency Virus Type 1 Replication in Microglial Cells
    • Rohr, O.; Lecestre, D.; Chasserot-Golaz, S.; Marban, C.; Avram, D.; Aunis, D.; Leid, M.; Schaeffer, E. Recruitment of Tat to Heterochromatin Protein HP1 via Interaction with CTIP2 Inhibits Human Immunodeficiency Virus Type 1 Replication in Microglial Cells J. Virol. 2003, 77, 5415-5427
    • (2003) J. Virol. , vol.77 , pp. 5415-5427
    • Rohr, O.1    Lecestre, D.2    Chasserot-Golaz, S.3    Marban, C.4    Avram, D.5    Aunis, D.6    Leid, M.7    Schaeffer, E.8
  • 39
    • 0242322010 scopus 로고    scopus 로고
    • Involvement of the Histone Deacetylase SIRT1 in Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF)-Interacting Protein 2-Mediated Transcriptional Repression
    • Senawong, T.; Peterson, V. J.; Avram, D.; Shepherd, D. M.; Frye, R. A.; Minucci, S.; Leid, M. Involvement of the Histone Deacetylase SIRT1 in Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF)-Interacting Protein 2-Mediated Transcriptional Repression J. Biol. Chem. 2003, 278, 43041-43050
    • (2003) J. Biol. Chem. , vol.278 , pp. 43041-43050
    • Senawong, T.1    Peterson, V.J.2    Avram, D.3    Shepherd, D.M.4    Frye, R.A.5    Minucci, S.6    Leid, M.7
  • 46
    • 78049274795 scopus 로고    scopus 로고
    • Timing Control in Regulatory Networks by Multisite Protein Modifications
    • Salazar, C.; Brümmer, A.; Alberghina, L.; Höfer, T. Timing Control in Regulatory Networks by Multisite Protein Modifications Trends Cell Biol. 2010, 20, 634-641
    • (2010) Trends Cell Biol. , vol.20 , pp. 634-641
    • Salazar, C.1    Brümmer, A.2    Alberghina, L.3    Höfer, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.