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Volumn 587, Issue 11, 2013, Pages 1587-1591

Stochastic machines as a colocalization mechanism for scaffold protein function

Author keywords

Molecular machines; Protein complexes; Scaffold proteins; Signaling

Indexed keywords

AXIN; BETA CATENIN; CASEIN KINASE IALPHA; GLYCOGEN SYNTHASE KINASE 3BETA; SCAFFOLD PROTEIN; WNT PROTEIN;

EID: 84878224022     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.04.006     Document Type: Article
Times cited : (40)

References (39)
  • 1
    • 0031457978 scopus 로고    scopus 로고
    • The mouse fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation
    • L. Zeng The mouse fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation Cell 90 1997 181 192
    • (1997) Cell , vol.90 , pp. 181-192
    • Zeng, L.1
  • 2
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta
    • M.J. Hart, R. de los Santos, I.N. Albert, B. Rubinfeld, and P. Polakis Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta Curr. Biol. 8 1998 573 581
    • (1998) Curr. Biol. , vol.8 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 3
    • 0037155691 scopus 로고    scopus 로고
    • Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism
    • C. Liu Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism Cell 108 2002 837 847
    • (2002) Cell , vol.108 , pp. 837-847
    • Liu, C.1
  • 4
    • 0037124056 scopus 로고    scopus 로고
    • Casein kinase i and casein kinase II differentially regulate Axin function in Wnt and JNK pathways
    • Y. Zhang, W.J. Qiu, S.C. Chan, J. Han, X. He, and S.C. Lin Casein kinase I and casein kinase II differentially regulate Axin function in Wnt and JNK pathways J. Biol. Chem. 277 2002 17706 17712
    • (2002) J. Biol. Chem. , vol.277 , pp. 17706-17712
    • Zhang, Y.1    Qiu, W.J.2    Chan, S.C.3    Han, J.4    He, X.5    Lin, S.C.6
  • 6
    • 0037415737 scopus 로고    scopus 로고
    • Structural basis for recruitment of glycogen synthase kinase 3beta to the Axin-APC scaffold complex
    • R. Dajani, E. Fraser, S.M. Roe, M. Yeo, V.M. Good, V. Thompson, T.C. Dale, and L.H. Pearl Structural basis for recruitment of glycogen synthase kinase 3beta to the Axin-APC scaffold complex EMBO J. 22 2003 494 501
    • (2003) EMBO J. , vol.22 , pp. 494-501
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Yeo, M.4    Good, V.M.5    Thompson, V.6    Dale, T.C.7    Pearl, L.H.8
  • 7
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • J. Kuriyan, and D. Eisenberg The origin of protein interactions and allostery in colocalization Nature 450 2007 983 990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 8
    • 50049097448 scopus 로고    scopus 로고
    • Intrinsic disorder in scaffold proteins: Getting more from less
    • M.S. Cortese, V.N. Uversky, and A.K. Dunker Intrinsic disorder in scaffold proteins: getting more from less Prog. Biophys. Mol. Biol. 98 2008 85 106
    • (2008) Prog. Biophys. Mol. Biol. , vol.98 , pp. 85-106
    • Cortese, M.S.1    Uversky, V.N.2    Dunker, A.K.3
  • 9
    • 79952114716 scopus 로고    scopus 로고
    • Functional classification of scaffold proteins and related molecules
    • L. Buday, and P. Tompa Functional classification of scaffold proteins and related molecules FEBS J. 277 2010 4348 4355
    • (2010) FEBS J. , vol.277 , pp. 4348-4355
    • Buday, L.1    Tompa, P.2
  • 10
    • 0033054464 scopus 로고    scopus 로고
    • The oncogenic activation of beta-catenin
    • P. Polakis The oncogenic activation of beta-catenin Curr. Opin. Genet. Dev. 9 1999 15 21
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 15-21
    • Polakis, P.1
  • 12
    • 84863518014 scopus 로고    scopus 로고
    • MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins
    • F.M. Disfani, W.L. Hsu, M.J. Mizianty, C.J. Oldfield, B. Xue, A.K. Dunker, V.N. Uversky, and L. Kurgan MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins Bioinformatics 28 2012 i75 i83
    • (2012) Bioinformatics , vol.28
    • Disfani, F.M.1    Hsu, W.L.2    Mizianty, M.J.3    Oldfield, C.J.4    Xue, B.5    Dunker, A.K.6    Uversky, V.N.7    Kurgan, L.8
  • 14
  • 15
    • 0034708763 scopus 로고    scopus 로고
    • Down-regulation of beta-catenin by the colorectal tumor suppressor APC requires association with Axin and beta-catenin
    • K. Kawahara, T. Morishita, T. Nakamura, F. Hamada, K. Toyoshima, and T. Akiyama Down-regulation of beta-catenin by the colorectal tumor suppressor APC requires association with Axin and beta-catenin J. Biol. Chem. 275 2000 8369 8374
    • (2000) J. Biol. Chem. , vol.275 , pp. 8369-8374
    • Kawahara, K.1    Morishita, T.2    Nakamura, T.3    Hamada, F.4    Toyoshima, K.5    Akiyama, T.6
  • 16
    • 84859320307 scopus 로고    scopus 로고
    • The roles of intrinsic disorder in orchestrating the Wnt-pathway
    • B. Xue, A.K. Dunker, and V.N. Uversky The roles of intrinsic disorder in orchestrating the Wnt-pathway J. Biomol. Struct. Dyn. 29 2012 843 861
    • (2012) J. Biomol. Struct. Dyn. , vol.29 , pp. 843-861
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 18
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: A critical assessment of the "fly-casting" mechanism
    • Y. Huang, and Z. Liu Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism J. Mol. Biol. 393 2009 1143 1159
    • (2009) J. Mol. Biol. , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2
  • 19
    • 84864585933 scopus 로고    scopus 로고
    • Corrigendum to "kinetic advantage of intrinsically disordered proteins in coupled folding-bindign process: A critical assessment of the "fly-casting" mechanism." [J. Mol. Biol. 393 (2009) 1143-1159]
    • Y. Huang, and Z. Liu Corrigendum to "Kinetic advantage of intrinsically disordered proteins in coupled folding-bindign process: a critical assessment of the "fly-casting" mechanism." [J. Mol. Biol. 393 (2009) 1143-1159] J. Mol. Biol. 422 2012 156
    • (2012) J. Mol. Biol. , vol.422 , pp. 156
    • Huang, Y.1    Liu, Z.2
  • 20
    • 77956332835 scopus 로고    scopus 로고
    • Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators
    • J.A. Marsh, B. Dancheck, M.J. Ragusa, M. Allaire, J.D. Forman-Kay, and W. Peti Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators Structure 18 2010 1094 1103
    • (2010) Structure , vol.18 , pp. 1094-1103
    • Marsh, J.A.1    Dancheck, B.2    Ragusa, M.J.3    Allaire, M.4    Forman-Kay, J.D.5    Peti, W.6
  • 21
    • 82655179901 scopus 로고    scopus 로고
    • Order and disorder in large multi-site docking proteins of the Gab family - Implications for signalling complex formation and inhibitor design strategies
    • P.C. Simister, and S.M. Feller Order and disorder in large multi-site docking proteins of the Gab family - implications for signalling complex formation and inhibitor design strategies Mol. BioSyst. 8 2012 33 46
    • (2012) Mol. BioSyst. , vol.8 , pp. 33-46
    • Simister, P.C.1    Feller, S.M.2
  • 22
    • 79952259103 scopus 로고    scopus 로고
    • Self-organization and regulation of intrinsically disordered proteins with folded N-termini
    • P.C. Simister, F. Schaper, N. O'Reilly, S. McGowan, and S.M. Feller Self-organization and regulation of intrinsically disordered proteins with folded N-termini PLoS Biol. 9 2011 e1000591
    • (2011) PLoS Biol. , vol.9 , pp. 1000591
    • Simister, P.C.1    Schaper, F.2    O'Reilly, N.3    McGowan, S.4    Feller, S.M.5
  • 23
    • 78650858373 scopus 로고    scopus 로고
    • Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded
    • M. Noutsou Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded J. Mol. Biol. 405 2011 773 786
    • (2011) J. Mol. Biol. , vol.405 , pp. 773-786
    • Noutsou, M.1
  • 24
    • 34249930064 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of the axin DIX domain
    • N. Shibata Crystallization and preliminary X-ray crystallographic studies of the axin DIX domain Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 63 2007 529 531
    • (2007) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.63 , pp. 529-531
    • Shibata, N.1
  • 25
    • 0028218683 scopus 로고
    • Modular arrangement of proteins as inferred from analysis of homology
    • E.L. Sonnhammer, and D. Kahn Modular arrangement of proteins as inferred from analysis of homology Protein Sci. 3 1994 482 492
    • (1994) Protein Sci. , vol.3 , pp. 482-492
    • Sonnhammer, E.L.1    Kahn, D.2
  • 26
    • 0023653232 scopus 로고
    • The Drosophila homolog of the mouse mammary oncogene int-1 is identical to the segment polarity gene wingless
    • F. Rijsewijk, M. Schuermann, E. Wagenaar, P. Parren, D. Weigel, and R. Nusse The Drosophila homolog of the mouse mammary oncogene int-1 is identical to the segment polarity gene wingless Cell 50 1987 649 657
    • (1987) Cell , vol.50 , pp. 649-657
    • Rijsewijk, F.1    Schuermann, M.2    Wagenaar, E.3    Parren, P.4    Weigel, D.5    Nusse, R.6
  • 27
    • 0017105003 scopus 로고
    • Effect of the Wingless (wg1) mutation on wing and haltere development in Drosophila melanogaster
    • R.P. Sharma, and V.L. Chopra Effect of the Wingless (wg1) mutation on wing and haltere development in Drosophila melanogaster Dev. Biol. 48 1976 461 465
    • (1976) Dev. Biol. , vol.48 , pp. 461-465
    • Sharma, R.P.1    Chopra, V.L.2
  • 28
    • 0019133661 scopus 로고
    • Mutations affecting segment number and polarity in Drosophila
    • C. Nusslein-Volhard, and E. Wieschaus Mutations affecting segment number and polarity in Drosophila Nature 287 1980 795 801
    • (1980) Nature , vol.287 , pp. 795-801
    • Nusslein-Volhard, C.1    Wieschaus, E.2
  • 29
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: Components, mechanisms, and diseases
    • B.T. MacDonald, K. Tamai, and X. He Wnt/beta-catenin signaling: components, mechanisms, and diseases Dev. Cell 17 2009 9 26
    • (2009) Dev. Cell , vol.17 , pp. 9-26
    • Macdonald, B.T.1    Tamai, K.2    He, X.3
  • 30
    • 78650153738 scopus 로고    scopus 로고
    • Musite, a tool for global prediction of general and kinase-specific phosphorylation sites
    • J. Gao, J.J. Thelen, A.K. Dunker, and D. Xu Musite, a tool for global prediction of general and kinase-specific phosphorylation sites Mol. Cell. Proteomics 9 2010 2586 2600
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2586-2600
    • Gao, J.1    Thelen, J.J.2    Dunker, A.K.3    Xu, D.4
  • 33
    • 79951850741 scopus 로고    scopus 로고
    • Defining the geometry of the two-component proteasome degron
    • T. Inobe, S. Fishbain, S. Prakash, and A. Matouschek Defining the geometry of the two-component proteasome degron Nat. Chem. Biol. 7 2011 161 167
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 161-167
    • Inobe, T.1    Fishbain, S.2    Prakash, S.3    Matouschek, A.4
  • 35
    • 38149104520 scopus 로고    scopus 로고
    • Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha
    • E.J. Sacho, F.A. Kadyrov, P. Modrich, T.A. Kunkel, and D.A. Erie Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha Mol. Cell 29 2008 112 121
    • (2008) Mol. Cell , vol.29 , pp. 112-121
    • Sacho, E.J.1    Kadyrov, F.A.2    Modrich, P.3    Kunkel, T.A.4    Erie, D.A.5
  • 37
    • 0019872903 scopus 로고
    • Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide
    • J.H. Rosa, and F.M. Richards Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide J. Mol. Biol. 145 1981 835 851
    • (1981) J. Mol. Biol. , vol.145 , pp. 835-851
    • Rosa, J.H.1    Richards, F.M.2
  • 38
    • 84859701551 scopus 로고    scopus 로고
    • Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life
    • B. Xue, A.K. Dunker, and V.N. Uversky Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life J. Biomol. Struct. Dyn. 30 2012 137 149
    • (2012) J. Biomol. Struct. Dyn. , vol.30 , pp. 137-149
    • Xue, B.1    Dunker, A.K.2    Uversky, V.N.3
  • 39
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • B. Alberts The cell as a collection of protein machines: preparing the next generation of molecular biologists Cell 92 1998 291 294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1


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