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Volumn 109, Issue 51, 2012, Pages 20865-20870

Mechanism of CREB recognition and coactivation by the CREB-regulated transcriptional coactivator CRTC2

Author keywords

Cellular signaling; Protein protein interaction; Transcription regulation

Indexed keywords

BASIC LEUCINE ZIPPER TRANSCRIPTION FACTOR; CYCLIC AMP; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; MONOMER;

EID: 84871364913     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1219028109     Document Type: Article
Times cited : (70)

References (41)
  • 1
    • 33646157076 scopus 로고    scopus 로고
    • Deciphering B-ZIP transcription factor interactions in vitro and in vivo
    • Vinson C, Acharya A, Taparowsky EJ (2006) Deciphering B-ZIP transcription factor interactions in vitro and in vivo. Biochim Biophys Acta 1759(1-2):4-12.
    • (2006) Biochim Biophys Acta , vol.1759 , Issue.1-2 , pp. 4-12
    • Vinson, C.1    Acharya, A.2    Taparowsky, E.J.3
  • 2
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • Montminy M (1997) Transcriptional regulation by cyclic AMP. Annu Rev Biochem 66:807-822.
    • (1997) Annu Rev Biochem , vol.66 , pp. 807-822
    • Montminy, M.1
  • 3
    • 79951962147 scopus 로고    scopus 로고
    • CREB and the CRTC co-activators: Sensors for hormonal and metabolic signals
    • Altarejos JY, Montminy M (2011) CREB and the CRTC co-activators: Sensors for hormonal and metabolic signals. Nat Rev Mol Cell Biol 12(3):141-151.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.3 , pp. 141-151
    • Altarejos, J.Y.1    Montminy, M.2
  • 4
    • 0027433708 scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • Chrivia JC, et al. (1993) Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 365(6449):855-859.
    • (1993) Nature , vol.365 , Issue.6449 , pp. 855-859
    • Chrivia, J.C.1
  • 5
    • 0141922981 scopus 로고    scopus 로고
    • TORCs: Transducers of regulated CREB activity
    • Conkright MD, et al. (2003) TORCs: Transducers of regulated CREB activity. Mol Cell 12 (2):413-423.
    • (2003) Mol Cell , vol.12 , Issue.2 , pp. 413-423
    • Conkright, M.D.1
  • 6
    • 0142091390 scopus 로고    scopus 로고
    • Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells
    • Iourgenko V, et al. (2003) Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. Proc Natl Acad Sci USA 100(21):12147-12152.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.21 , pp. 12147-12152
    • Iourgenko, V.1
  • 7
    • 5344228270 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector
    • Screaton RA, et al. (2004) The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. Cell 119(1):61-74.
    • (2004) Cell , vol.119 , Issue.1 , pp. 61-74
    • Screaton, R.A.1
  • 8
    • 55149088605 scopus 로고    scopus 로고
    • Requirement of TORC1 for late-phase long-term potentiation in the hippocampus
    • Zhou Y, et al. (2006) Requirement of TORC1 for late-phase long-term potentiation in the hippocampus. PLoS ONE 1:e16.
    • (2006) PLoS ONE , vol.1
    • Zhou, Y.1
  • 9
    • 34248388957 scopus 로고    scopus 로고
    • TORC1 is a calcium- and cAMP-sensitive coincidence detector involved in hippocampal long-term synaptic plasticity
    • Kovács KA, et al. (2007) TORC1 is a calcium- and cAMP-sensitive coincidence detector involved in hippocampal long-term synaptic plasticity. Proc Natl Acad Sci USA 104(11):4700-4705.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.11 , pp. 4700-4705
    • Kovács, K.A.1
  • 10
    • 27144506185 scopus 로고    scopus 로고
    • The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism
    • Koo SH, et al. (2005) The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism. Nature 437(7062):1109-1111.
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1109-1111
    • Koo, S.H.1
  • 11
    • 42649140573 scopus 로고    scopus 로고
    • The insulin-regulated CREB coactivator TORC promotes stress resistance in Drosophila
    • Wang B, et al. (2008) The insulin-regulated CREB coactivator TORC promotes stress resistance in Drosophila. Cell Metab 7(5):434-444.
    • (2008) Cell Metab , vol.7 , Issue.5 , pp. 434-444
    • Wang, B.1
  • 12
    • 79951787452 scopus 로고    scopus 로고
    • Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB
    • MairW, et al. (2011) Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB. Nature 470(7334):404-408.
    • (2011) Nature , vol.470 , Issue.7334 , pp. 404-408
    • Mair, W.1
  • 13
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions
    • Radhakrishnan I, et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions. Cell 91(6):741-752.
    • (1997) Cell , vol.91 , Issue.6 , pp. 741-752
    • Radhakrishnan, I.1
  • 14
    • 34249941195 scopus 로고    scopus 로고
    • A fundamental system of cellular energy homeostasis regulated by PGC-1alpha
    • Rohas LM, et al. (2007) A fundamental system of cellular energy homeostasis regulated by PGC-1alpha. Proc Natl Acad Sci USA 104(19):7933-7938.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.19 , pp. 7933-7938
    • Rohas, L.M.1
  • 15
    • 20144379523 scopus 로고    scopus 로고
    • Genome-wide analysis of cAMP-response element binding protein occupancy, phosphorylation, and target gene activation in human tissues
    • Zhang X, et al. (2005) Genome-wide analysis of cAMP-response element binding protein occupancy, phosphorylation, and target gene activation in human tissues. Proc Natl Acad Sci USA 102(12):4459-4464.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.12 , pp. 4459-4464
    • Zhang, X.1
  • 16
    • 0034634671 scopus 로고    scopus 로고
    • The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding
    • Schumacher MA, Goodman RH, Brennan RG (2000) The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding. J Biol Chem 275(45):35242-35247.
    • (2000) J Biol Chem , vol.275 , Issue.45 , pp. 35242-35247
    • Schumacher, M.A.1    Goodman, R.H.2    Brennan, R.G.3
  • 17
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • Buck M (1998) Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins. Q Rev Biophys 31(3):297-355.
    • (1998) Q Rev Biophys , vol.31 , Issue.3 , pp. 297-355
    • Buck, M.1
  • 18
    • 0035853761 scopus 로고    scopus 로고
    • Consensus and variant cAMP-regulated enhancers have distinct CREB-binding properties
    • Craig JC, et al. (2001) Consensus and variant cAMP-regulated enhancers have distinct CREB-binding properties. J Biol Chem 276(15):11719-11728.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 11719-11728
    • Craig, J.C.1
  • 19
    • 0024370748 scopus 로고
    • Scissors-grip model for DNA recognition by a family of leucine zipper proteins
    • Vinson CR, Sigler PB, McKnight SL (1989) Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science 246(4932):911-916.
    • (1989) Science , vol.246 , Issue.4932 , pp. 911-916
    • Vinson, C.R.1    Sigler, P.B.2    McKnight, S.L.3
  • 20
    • 84855563516 scopus 로고    scopus 로고
    • Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway
    • Jeong H, et al. (2012) Sirt1 mediates neuroprotection from mutant huntingtin by activation of the TORC1 and CREB transcriptional pathway. Nat Med 18(1):159-165.
    • (2012) Nat Med , vol.18 , Issue.1 , pp. 159-165
    • Jeong, H.1
  • 21
    • 0036829096 scopus 로고    scopus 로고
    • Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    • Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE (2002) Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J Biol Chem 277(44):42241-42248.
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 42241-42248
    • Zor, T.1    Mayr, B.M.2    Dyson, H.J.3    Montminy, M.R.4    Wright, P.E.5
  • 22
    • 30744455255 scopus 로고    scopus 로고
    • A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons
    • Riccio A, et al. (2006) A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons. Mol Cell 21(2):283-294.
    • (2006) Mol Cell , vol.21 , Issue.2 , pp. 283-294
    • Riccio, A.1
  • 23
    • 0035798407 scopus 로고    scopus 로고
    • Two cysteine residues in the DNA-binding domain of CREB control binding to CRE and CREB-mediated gene expression
    • Goren I, Tavor E, Goldblum A, Honigman A (2001) Two cysteine residues in the DNA-binding domain of CREB control binding to CRE and CREB-mediated gene expression. J Mol Biol 313(4):695-709.
    • (2001) J Mol Biol , vol.313 , Issue.4 , pp. 695-709
    • Goren, I.1    Tavor, E.2    Goldblum, A.3    Honigman, A.4
  • 24
    • 1242293658 scopus 로고    scopus 로고
    • A pivotal role of cyclic AMP-responsive element binding protein in tumor progression
    • Abramovitch R, et al. (2004) A pivotal role of cyclic AMP-responsive element binding protein in tumor progression. Cancer Res 64(4):1338-1346.
    • (2004) Cancer Res , vol.64 , Issue.4 , pp. 1338-1346
    • Abramovitch, R.1
  • 25
    • 53349143521 scopus 로고    scopus 로고
    • A key role for cyclic AMP-responsive element binding protein in hypoxia-mediated activation of the angiogenesis factor CCN1 (CYR61) in tumor cells
    • Meyuhas R, et al. (2008) A key role for cyclic AMP-responsive element binding protein in hypoxia-mediated activation of the angiogenesis factor CCN1 (CYR61) in tumor cells. Mol Cancer Res 6(9):1397-1409.
    • (2008) Mol Cancer Res , vol.6 , Issue.9 , pp. 1397-1409
    • Meyuhas, R.1
  • 26
    • 0026725132 scopus 로고
    • Human T-cell lymphotropic virus type i (HTLV-I) transcriptional activator, Tax, enhances CREB binding to HTLV-I 21-base-pair repeats by protein-protein interaction
    • Zhao LJ, Giam CZ (1992) Human T-cell lymphotropic virus type I (HTLV-I) transcriptional activator, Tax, enhances CREB binding to HTLV-I 21-base-pair repeats by protein-protein interaction. Proc Natl Acad Sci USA 89(15):7070-7074.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.15 , pp. 7070-7074
    • Zhao, L.J.1    Giam, C.Z.2
  • 27
    • 0029123022 scopus 로고
    • Mechanism of DNA-binding enhancement by the human T-cell leukaemia virus transactivator Tax
    • Baranger AM, et al. (1995) Mechanism of DNA-binding enhancement by the human T-cell leukaemia virus transactivator Tax. Nature 376(6541):606-608.
    • (1995) Nature , vol.376 , Issue.6541 , pp. 606-608
    • Baranger, A.M.1
  • 28
    • 77949273352 scopus 로고    scopus 로고
    • The HTLV-1 Tax protein: Revealing mechanisms of transcriptional activation through histone acetylation and nucleosome disassembly
    • Nyborg JK, Egan D, Sharma N (2010) The HTLV-1 Tax protein: Revealing mechanisms of transcriptional activation through histone acetylation and nucleosome disassembly. Biochim Biophys Acta 1799(3-4):266-274.
    • (2010) Biochim Biophys Acta , vol.1799 , Issue.3-4 , pp. 266-274
    • Nyborg, J.K.1    Egan, D.2    Sharma, N.3
  • 29
    • 0343811676 scopus 로고    scopus 로고
    • Mechanism of DNA binding enhancement by hepatitis B virus protein pX
    • Palmer CR, Gegnas LD, Schepartz A (1997) Mechanism of DNA binding enhancement by hepatitis B virus protein pX. Biochemistry 36(49):15349-15355.
    • (1997) Biochemistry , vol.36 , Issue.49 , pp. 15349-15355
    • Palmer, C.R.1    Gegnas, L.D.2    Schepartz, A.3
  • 30
    • 33746988776 scopus 로고    scopus 로고
    • Differential gene regulation by selective association of transcriptional coactivators and bZIP DNA-binding domains
    • Miotto B, Struhl K (2006) Differential gene regulation by selective association of transcriptional coactivators and bZIP DNA-binding domains. Mol Cell Biol 26(16):5969-5982.
    • (2006) Mol Cell Biol , vol.26 , Issue.16 , pp. 5969-5982
    • Miotto, B.1    Struhl, K.2
  • 31
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols L, et al. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr Purif 25(1):8-15.
    • (2002) Protein Expr Purif , vol.25 , Issue.1 , pp. 8-15
    • Stols, L.1
  • 32
    • 0034465455 scopus 로고    scopus 로고
    • Synergistic activation of the inhibin alpha-promoter by steroidogenic factor-1 and cyclic adenosine 3′,5′-monophosphate
    • Ito M, Park Y, Weck J, Mayo KE, Jameson JL (2000) Synergistic activation of the inhibin alpha-promoter by steroidogenic factor-1 and cyclic adenosine 3′,5′-monophosphate. Mol Endocrinol 14(1):66-81.
    • (2000) Mol Endocrinol , vol.14 , Issue.1 , pp. 66-81
    • Ito, M.1    Park, Y.2    Weck, J.3    Mayo, K.E.4    Jameson, J.L.5
  • 33
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182(2):319-326.
    • (1989) Anal Biochem , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 34
    • 1042300247 scopus 로고    scopus 로고
    • Fluorescence anisotropy assays for analysis of ISWI-DNA and ISWI-nucleosome interactions
    • Chin J, Längst G, Becker PB, Widom J (2004) Fluorescence anisotropy assays for analysis of ISWI-DNA and ISWI-nucleosome interactions. Methods Enzymol 376:3-16.
    • (2004) Methods Enzymol , vol.376 , pp. 3-16
    • Chin, J.1    Längst, G.2    Becker, P.B.3    Widom, J.4
  • 35
    • 77649253906 scopus 로고    scopus 로고
    • Targeted disruption of the CREB coactivator Crtc2 increases insulin sensitivity
    • Wang Y, et al. (2010) Targeted disruption of the CREB coactivator Crtc2 increases insulin sensitivity. Proc Natl Acad Sci USA 107(7):3087-3092.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.7 , pp. 3087-3092
    • Wang, Y.1
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6(5):458-463.
    • (1999) Nat Struct Biol , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 57(Pt 1):122-133.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , Issue.PART 1 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 41
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS, Thornton JM (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231(4):1049-1067.
    • (1993) J Mol Biol , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3


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