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Volumn 1813, Issue 5, 2011, Pages 1050-1058

Sumoylation regulates nuclear localization of repressor DREAM

Author keywords

DREAM; KChIPs; Nuclear localization; SUMO; Trigeminal neuron; Ubc9

Indexed keywords

CALSENILIN; PROTEIN UBC9;

EID: 79955648513     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.11.001     Document Type: Article
Times cited : (23)

References (40)
  • 2
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson E.S. Protein modification by SUMO. Annu. Rev. Biochem. 2004, 73:355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 5
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro J.M., Thomson J., Hay R.T. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 1997, 417:297-300.
    • (1997) FEBS Lett. , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 6
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: a history of modification
    • Hay R.T. SUMO: a history of modification. Mol. Cell 2005, 18:1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 7
    • 33747838835 scopus 로고    scopus 로고
    • SUMOsp: a web server for sumoylation site prediction
    • Xue Y., Zhou F., Fu C., Xu Y., Yao X. SUMOsp: a web server for sumoylation site prediction. Nucleic Acids Res. 2006, 34:W254-257.
    • (2006) Nucleic Acids Res. , vol.34
    • Xue, Y.1    Zhou, F.2    Fu, C.3    Xu, Y.4    Yao, X.5
  • 8
    • 33748416853 scopus 로고    scopus 로고
    • A recurrent phospho-sumoyl switch in transcriptional repression and beyond
    • Yang X.J., Gregoire S. A recurrent phospho-sumoyl switch in transcriptional repression and beyond. Mol. Cell 2006, 23:779-786.
    • (2006) Mol. Cell , vol.23 , pp. 779-786
    • Yang, X.J.1    Gregoire, S.2
  • 12
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • Buxbaum J.D., Choi E.K., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E., Wasco W. Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nat. Med. 1998, 4:1177-1181.
    • (1998) Nat. Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.K.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6    Wasco, W.7
  • 15
    • 33847281052 scopus 로고    scopus 로고
    • Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is mediated by calsenilin
    • Chang J.W., Choi H., Kim H.J., Jo D.G., Jeon Y.J., Noh J.Y., Park W.J., Jung Y.K. Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is mediated by calsenilin. Hum. Mol. Genet. 2007, 16:317-326.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 317-326
    • Chang, J.W.1    Choi, H.2    Kim, H.J.3    Jo, D.G.4    Jeon, Y.J.5    Noh, J.Y.6    Park, W.J.7    Jung, Y.K.8
  • 17
    • 2042496266 scopus 로고    scopus 로고
    • Intracellular calcium modulates the nuclear translocation of calsenilin
    • Zaidi N.F., Thomson E.E., Choi E.K., Buxbaum J.D., Wasco W. Intracellular calcium modulates the nuclear translocation of calsenilin. J. Neurochem. 2004, 89:593-601.
    • (2004) J. Neurochem. , vol.89 , pp. 593-601
    • Zaidi, N.F.1    Thomson, E.E.2    Choi, E.K.3    Buxbaum, J.D.4    Wasco, W.5
  • 19
    • 0023836862 scopus 로고
    • Dissociation of c-fos from ODC expression and neuronal differentiation in a PC12 subline stably transfected with an inducible N-ras oncogene
    • Guerrero I., Pellicer A., Burstein D.E. Dissociation of c-fos from ODC expression and neuronal differentiation in a PC12 subline stably transfected with an inducible N-ras oncogene. Biochem. Biophys. Res. Commun. 1988, 150:1185-1192.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 1185-1192
    • Guerrero, I.1    Pellicer, A.2    Burstein, D.E.3
  • 20
    • 23944487202 scopus 로고    scopus 로고
    • In nucleo enzymatic assays for the identification and characterization of histone modifying activities
    • Fischle W. In nucleo enzymatic assays for the identification and characterization of histone modifying activities. Methods 2005, 36:362-367.
    • (2005) Methods , vol.36 , pp. 362-367
    • Fischle, W.1
  • 21
    • 27144489025 scopus 로고    scopus 로고
    • Transcriptional repressor DREAM regulates T-lymphocyte proliferation and cytokine gene expression
    • Savignac M., Pintado B., Gutierrez-Adan A., Palczewska M., Mellstrom B., Naranjo J.R. Transcriptional repressor DREAM regulates T-lymphocyte proliferation and cytokine gene expression. EMBO J. 2005, 24:3555-3564.
    • (2005) EMBO J. , vol.24 , pp. 3555-3564
    • Savignac, M.1    Pintado, B.2    Gutierrez-Adan, A.3    Palczewska, M.4    Mellstrom, B.5    Naranjo, J.R.6
  • 22
    • 0035809126 scopus 로고    scopus 로고
    • Neuronal body size correlates with the number of nucleoli and Cajal bodies, and with the organization of the splicing machinery in rat trigeminal ganglion neurons
    • Pena E., Berciano M.T., Fernandez R., Ojeda J.L., Lafarga M. Neuronal body size correlates with the number of nucleoli and Cajal bodies, and with the organization of the splicing machinery in rat trigeminal ganglion neurons. J. Comp. Neurol. 2001, 430:250-263.
    • (2001) J. Comp. Neurol. , vol.430 , pp. 250-263
    • Pena, E.1    Berciano, M.T.2    Fernandez, R.3    Ojeda, J.L.4    Lafarga, M.5
  • 24
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • 29
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990, 8:52-56. 29.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 25
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 2003, 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 27
    • 1342333776 scopus 로고    scopus 로고
    • Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels
    • Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S. Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels. Neuron 2004, 41:573-586.
    • (2004) Neuron , vol.41 , pp. 573-586
    • Zhou, W.1    Qian, Y.2    Kunjilwar, K.3    Pfaffinger, P.J.4    Choe, S.5
  • 28
    • 39749113856 scopus 로고    scopus 로고
    • NMR structure of DREAM: implications for Ca(2+)-dependent DNA binding and protein dimerization
    • Lusin J.D., Vanarotti M., Li C., Valiveti A., Ames J.B. NMR structure of DREAM: implications for Ca(2+)-dependent DNA binding and protein dimerization. Biochemistry 2008, 47:2252-2264.
    • (2008) Biochemistry , vol.47 , pp. 2252-2264
    • Lusin, J.D.1    Vanarotti, M.2    Li, C.3    Valiveti, A.4    Ames, J.B.5
  • 29
  • 30
    • 0037205044 scopus 로고    scopus 로고
    • Signaling pathways for PC12 cell differentiation: making the right connections
    • Vaudry D., Stork P.J., Lazarovici P., Eiden L.E. Signaling pathways for PC12 cell differentiation: making the right connections. Science 2002, 296:1648-1649.
    • (2002) Science , vol.296 , pp. 1648-1649
    • Vaudry, D.1    Stork, P.J.2    Lazarovici, P.3    Eiden, L.E.4
  • 33
    • 0346665903 scopus 로고    scopus 로고
    • Regional and cellular distribution of DREAM in adult rat brain consistent with multiple sensory processing roles
    • Hammond P.I., Craig T.A., Kumar R., Brimijoin S. Regional and cellular distribution of DREAM in adult rat brain consistent with multiple sensory processing roles. Brain Res. Mol. Brain Res. 2003, 111:104-110.
    • (2003) Brain Res. Mol. Brain Res. , vol.111 , pp. 104-110
    • Hammond, P.I.1    Craig, T.A.2    Kumar, R.3    Brimijoin, S.4
  • 34
    • 33646514631 scopus 로고    scopus 로고
    • Nuclear organization and dynamics of transcription sites in rat sensory ganglia neurons detected by incorporation of 5'-fluorouridine into nascent RNA
    • Casafont I., Navascues J., Pena E., Lafarga M., Berciano M.T. Nuclear organization and dynamics of transcription sites in rat sensory ganglia neurons detected by incorporation of 5'-fluorouridine into nascent RNA. Neuroscience 2006, 140:453-462.
    • (2006) Neuroscience , vol.140 , pp. 453-462
    • Casafont, I.1    Navascues, J.2    Pena, E.3    Lafarga, M.4    Berciano, M.T.5
  • 35
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: a model for nuclear organelles
    • Lamond A.I., Spector D.L. Nuclear speckles: a model for nuclear organelles. Nat. Rev. Mol. Cell Biol. 2003, 4:605-612.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 36
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 1996, 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 37
    • 0032708680 scopus 로고    scopus 로고
    • Diversity of conformational states and changes within the EF-hand protein superfamily
    • Yap K.L., Ames J.B., Swindells M.B., Ikura M. Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins 1999, 37:499-507.
    • (1999) Proteins , vol.37 , pp. 499-507
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 38
    • 0036980146 scopus 로고    scopus 로고
    • 2+-binding proteins, recoverin and GCAP-2
    • 2+-binding proteins, recoverin and GCAP-2. Adv. Exp. Med. Biol. 2002, 514:333-348.
    • (2002) Adv. Exp. Med. Biol. , vol.514 , pp. 333-348
    • Ames, J.B.1    Ikura, M.2
  • 40
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 2000, 302:205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.