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Volumn 71, Issue 4, 2008, Pages 1686-1698

Huntingtin interacting protein HYPK is intrinsically unstructured

Author keywords

Huntington's disease; HYPK; IUP; Pre molten globule; Protein interaction

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); HUNTINGTIN; PAPAIN; TRYPSIN;

EID: 44349119206     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21856     Document Type: Article
Times cited : (24)

References (72)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993;72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
  • 3
    • 0037376680 scopus 로고    scopus 로고
    • Hickey MA, Chesselet MF. Apoptosis in Huntington's disease. Prog Neuro-Psychopharmacol Biol Psychiatry 2003;27:255-265.
    • Hickey MA, Chesselet MF. Apoptosis in Huntington's disease. Prog Neuro-Psychopharmacol Biol Psychiatry 2003;27:255-265.
  • 4
    • 0742323776 scopus 로고    scopus 로고
    • Mechanisms of cell death in polyglutamine expansion diseases
    • Lipinski MM, Yuan J. Mechanisms of cell death in polyglutamine expansion diseases. Curr Opin Pharmacol 2004;4:85-90.
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 85-90
    • Lipinski, M.M.1    Yuan, J.2
  • 5
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • Ross CA. Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 1997;19:1147-1150.
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 6
    • 0029082383 scopus 로고    scopus 로고
    • Duyao MP, Auerbach AB, Ryan A, Persichetti F, Barnes GT, McNeil SM, Ge P, Vonsattel JP, Gusella JF, Joyner AL. Inactivation of the mouse Huntington's disease gene homolog Hdh. Science 1995;269:407-410.
    • Duyao MP, Auerbach AB, Ryan A, Persichetti F, Barnes GT, McNeil SM, Ge P, Vonsattel JP, Gusella JF, Joyner AL. Inactivation of the mouse Huntington's disease gene homolog Hdh. Science 1995;269:407-410.
  • 9
    • 1242338861 scopus 로고    scopus 로고
    • Interrupting apoptosis in neurodegenerative disease: Potential for effective therapy?
    • Waldmeier PC, Tatton WG. Interrupting apoptosis in neurodegenerative disease: potential for effective therapy? Drug Discov Today 2004;9:210-218.
    • (2004) Drug Discov Today , vol.9 , pp. 210-218
    • Waldmeier, P.C.1    Tatton, W.G.2
  • 12
    • 34249715853 scopus 로고    scopus 로고
    • Kaltenbach LS, Romero E, Becklin RR, Chettier R, Bell R, Phansalkar A, Strand A, Torcassi C, Savage J, Hurlburt A, Cha GH, Ukani L, Chepanoske CL, Zhen Y, Sahasrabudhe S, Olson J, Kurschner C, Ellerby LM, Peltier JM, Botas J, Hughes RE. Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genetics 2007;3:e82(doi:10.1371/journal).
    • Kaltenbach LS, Romero E, Becklin RR, Chettier R, Bell R, Phansalkar A, Strand A, Torcassi C, Savage J, Hurlburt A, Cha GH, Ukani L, Chepanoske CL, Zhen Y, Sahasrabudhe S, Olson J, Kurschner C, Ellerby LM, Peltier JM, Botas J, Hughes RE. Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genetics 2007;3:e82(doi:10.1371/journal).
  • 13
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li SH, Li XJ. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 2004;20:146-154.
    • (2004) Trends Genet , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 14
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1α and heat shock protein 84 as aggregate-interacting proteins
    • Mitsui K, Nakayama H, Akagi T, Nekooki M, Ohtawa K, Takio K, Hashikawa T, Nukina N. Purification of polyglutamine aggregates and identification of elongation factor-1α and heat shock protein 84 as aggregate-interacting proteins. J Neurosci 2002;22:9267-9277.
    • (2002) J Neurosci , vol.22 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3    Nekooki, M.4    Ohtawa, K.5    Takio, K.6    Hashikawa, T.7    Nukina, N.8
  • 16
    • 0034649661 scopus 로고    scopus 로고
    • FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis
    • Hattula K, Peranen J. FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. Curr Biol 2000;10:1603-1606.
    • (2000) Curr Biol , vol.10 , pp. 1603-1606
    • Hattula, K.1    Peranen, J.2
  • 18
    • 0034284565 scopus 로고    scopus 로고
    • Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis
    • Passani AL, Bedford TM, Faber WP, McGinnis MK, Sharp HA, Gusella FJ, Vonsattel J, MacDonald ME. Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis. Hum Mol Genet 2000;9:2175-2182.
    • (2000) Hum Mol Genet , vol.9 , pp. 2175-2182
    • Passani, A.L.1    Bedford, T.M.2    Faber, W.P.3    McGinnis, M.K.4    Sharp, H.A.5    Gusella, F.J.6    Vonsattel, J.7    MacDonald, M.E.8
  • 21
    • 10444287633 scopus 로고    scopus 로고
    • Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins
    • Huang K, Yanai A, Kang R, Arstikaitis P, Singaraja RR, Metzler M, Mullard A, Haigh B, Gauthier-Campbell C. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 2004;44:977-986.
    • (2004) Neuron , vol.44 , pp. 977-986
    • Huang, K.1    Yanai, A.2    Kang, R.3    Arstikaitis, P.4    Singaraja, R.R.5    Metzler, M.6    Mullard, A.7    Haigh, B.8    Gauthier-Campbell, C.9
  • 22
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng Y, LeGall T, Oldfield CJ, Dunker AK, Uversky VN. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 2006;45:10448-10460.
    • (2006) Biochemistry , vol.45 , pp. 10448-10460
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 26
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002;11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 29
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero P, Obradovic Z, Dunker AK. Sequence data analysis for long disordered regions prediction in the calcineurin family. Genome Inform 1997;8:110-124.
    • (1997) Genome Inform , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 31
    • 34447539760 scopus 로고    scopus 로고
    • Composition profiler: A tool for discovery and visualization of amino acid composition differences
    • doi:10.1186/1471-2105-8-211
    • Vacic V, Uversky VN, Dunker AK, Lonardi S. Composition profiler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinform 2007;8:211. (doi:10.1186/1471-2105-8-211).
    • (2007) BMC Bioinform , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 32
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation: Application to crude preparations of sulfite and hydroxylamine reductases
    • Siegel LM, Monty KJ. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation: application to crude preparations of sulfite and hydroxylamine reductases. Biochim Biophys Acta 1966;112:346-362.
    • (1966) Biochim Biophys Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 34
    • 0037033042 scopus 로고    scopus 로고
    • A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function
    • Chakraborty A, Das I, Datta R, Sen B, Bhattacharyya D, Mandal C, Datta AK. A single-domain cyclophilin from Leishmania donovani reactivates soluble aggregates of adenosine kinase by isomerase-independent chaperone function. J Biol Chem 2002;277:47451-47460.
    • (2002) J Biol Chem , vol.277 , pp. 47451-47460
    • Chakraborty, A.1    Das, I.2    Datta, R.3    Sen, B.4    Bhattacharyya, D.5    Mandal, C.6    Datta, A.K.7
  • 36
    • 0029339760 scopus 로고    scopus 로고
    • Bhattacharyya K, Basak S. Somatostatin in a water-restricted environment: fluorescence and circular dichroism study in AOT reverse micelles. Photochem Photobiol 1995;62:17-23.
    • Bhattacharyya K, Basak S. Somatostatin in a water-restricted environment: fluorescence and circular dichroism study in AOT reverse micelles. Photochem Photobiol 1995;62:17-23.
  • 37
    • 6344280796 scopus 로고    scopus 로고
    • Recombinant EWS-FLI1 oncoprotein activates transcription
    • Üren A, Tcherkasskaya O, Toretsky JA. Recombinant EWS-FLI1 oncoprotein activates transcription. Biochemistry 2004;43:13579-13589.
    • (2004) Biochemistry , vol.43 , pp. 13579-13589
    • Üren, A.1    Tcherkasskaya, O.2    Toretsky, J.A.3
  • 38
    • 0344980717 scopus 로고    scopus 로고
    • Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin
    • Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Prot Struct Funct Genet 2003;53:855-862.
    • (2003) Prot Struct Funct Genet , vol.53 , pp. 855-862
    • Permyakov, S.E.1    Millett, I.S.2    Doniach, S.3    Permyakov, E.A.4    Uversky, V.N.5
  • 41
    • 0028980859 scopus 로고
    • 2+ responses of RBL-2H3 mast cells
    • 2+ responses of RBL-2H3 mast cells. Mol Biol Cell 1995;6:825-839.
    • (1995) Mol Biol Cell , vol.6 , pp. 825-839
    • Lee, R.J.1    Oliver, J.M.2
  • 44
    • 0021347987 scopus 로고
    • Tyrosine and tyrosinate fluorescence of bovine testes calmodulin: Calcium and pH dependence
    • Pundak S, Roche RS. Tyrosine and tyrosinate fluorescence of bovine testes calmodulin: calcium and pH dependence. Biochemistry 1984;23:1549-1555.
    • (1984) Biochemistry , vol.23 , pp. 1549-1555
    • Pundak, S.1    Roche, R.S.2
  • 45
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002;27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 46
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 50
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 51
    • 33644852931 scopus 로고    scopus 로고
    • One misfolded protein allows others to sneak by
    • Bates GP. One misfolded protein allows others to sneak by. Science 2006;311:1385-1386.
    • (2006) Science , vol.311 , pp. 1385-1386
    • Bates, G.P.1
  • 52
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P, Szász C, Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci 2005;30:484-489.
    • (2005) Trends Biochem Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szász, C.2    Buday, L.3
  • 53
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Prot Struct Funct Genet 2000;41:415-427.
    • (2000) Prot Struct Funct Genet , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 54
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999;293:321-323.
    • (1999) J Mol Biol , vol.293 , pp. 321-323
    • Dyson, H.J.1    Wright, P.E.2
  • 57
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models
    • Brandt R, Hundelt M, Shahani N. Tau alteration and neuronal degeneration in tauopathies: mechanisms and models. Biochim Biophys Acta 2005;1739:331-354.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 59
    • 0028170411 scopus 로고
    • Structural studies of Tau protein and Alzheimer paired helical filaments show no evidence for β-structure
    • Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E. Structural studies of Tau protein and Alzheimer paired helical filaments show no evidence for β-structure. J Biol Chem 1994;269:24290-24297.
    • (1994) J Biol Chem , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 60
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in α-synuclein fibril formation
    • Uversky VN, Li J, Fink AL. Evidence for a partially folded intermediate in α-synuclein fibril formation. J Biol Chem 2001;276:10737-10744.
    • (2001) J Biol Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 61
    • 0029904487 scopus 로고    scopus 로고
    • A protein implicated in Alzheimer's disease and learning is natively unfolded
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. NACP. A protein implicated in Alzheimer's disease and learning is natively unfolded. Biochemistry 1996;35:13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5    NACP6
  • 62
    • 0035824545 scopus 로고    scopus 로고
    • Residual structure and dynamics in Parkinson's disease-associated mutants of α-synuclein
    • Bussell R, Eliezer D. Residual structure and dynamics in Parkinson's disease-associated mutants of α-synuclein. J Biol Chem 2001;276:45996-46003.
    • (2001) J Biol Chem , vol.276 , pp. 45996-46003
    • Bussell, R.1    Eliezer, D.2
  • 63
    • 1942534598 scopus 로고    scopus 로고
    • Effects of parkinson's disease-linked mutations on the structure of lipid-associated α-synuclein
    • Bussell R, Eliezer D. Effects of parkinson's disease-linked mutations on the structure of lipid-associated α-synuclein Biochemistry 2004;43:4810-4818.
    • (2004) Biochemistry , vol.43 , pp. 4810-4818
    • Bussell, R.1    Eliezer, D.2
  • 64
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • Eliezer D, Kutluay E, Bussell R, Browne G. Conformational properties of α-synuclein in its free and lipid-associated states. J Mol Biol 2001;307:1061-1073.
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, R.3    Browne, G.4
  • 65
    • 0141677840 scopus 로고    scopus 로고
    • A Protein-chameleon: Conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky VN. A Protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders. J Biomol Struct Dyn 2003;21:211-234.
    • (2003) J Biomol Struct Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 66
    • 0037375786 scopus 로고    scopus 로고
    • Local protein unfolding and pathogenesis of polyglutamine- expansion diseases
    • Chen YW. Local protein unfolding and pathogenesis of polyglutamine- expansion diseases. Prot Struct Funct Genet 2003;51:68-73.
    • (2003) Prot Struct Funct Genet , vol.51 , pp. 68-73
    • Chen, Y.W.1
  • 68
    • 22144471491 scopus 로고    scopus 로고
    • Evidence for sequestration of polyglutamine inclusions by Drosophila myeloid leukemia factor
    • Kim WY, Fayazi Z, Bao X, Higgins D, Kazemi-Esfarjani P. Evidence for sequestration of polyglutamine inclusions by Drosophila myeloid leukemia factor. Mol Cell Neurosci 2005;29:536-544.
    • (2005) Mol Cell Neurosci , vol.29 , pp. 536-544
    • Kim, W.Y.1    Fayazi, Z.2    Bao, X.3    Higgins, D.4    Kazemi-Esfarjani, P.5
  • 69
    • 0036796287 scopus 로고    scopus 로고
    • Suppression of polyglutamine toxicity by a Drosophila homolog of myeloid leukemia factor 1
    • Kazemi-Esfarjani P, Benzer S. Suppression of polyglutamine toxicity by a Drosophila homolog of myeloid leukemia factor 1. Hum Mol Genet 2002;11:2657-72.
    • (2002) Hum Mol Genet , vol.11 , pp. 2657-2672
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 70
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, Mestril R, Mahal A, Smith DL, Woodman B, Bates GP. Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum Mol Genet 2004;13:1389-1405.
    • (2004) Hum Mol Genet , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 71
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H, Breuer P, Hayer-Hart MK, Hart FU. Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci USA 2002;99:16412-16418.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hart, M.K.3    Hart, F.U.4


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