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Volumn 74, Issue 1, 2009, Pages 104-121

Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution

Author keywords

Axonal transport; Circular dichroism; Limited proteolysis; Microtubular transport; Protein protein interactions; SAXS; Spectroscopy

Indexed keywords

CELL PROTEIN; PROTEIN FEZ1; PROTEIN KINASE C EPSILON; UNCLASSIFIED DRUG; CLASP2 PROTEIN, HUMAN; FEZ1 PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; NERVE PROTEIN; PEPTIDE FRAGMENT; PROTEIN KINASE C; PROTEIN KINASE C (19 31); PROTEIN KINASE C (19-31); RECOMBINANT PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 58949104029     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22135     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 0030965832 scopus 로고    scopus 로고
    • The Caenorhabditis elegans gene unc-76 and its human homologs define a new gene family involved in axonal outgrowth and fasciculation
    • Bloom L, Horvitz HR. The Caenorhabditis elegans gene unc-76 and its human homologs define a new gene family involved in axonal outgrowth and fasciculation. Proc Natl Acad Sci USA 1997;94:3414-3419.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3414-3419
    • Bloom, L.1    Horvitz, H.R.2
  • 3
    • 0033535042 scopus 로고    scopus 로고
    • Mammalian homologue of the Caenorhabditis elegans UNC-76 protein involved in axonal outgrowth is a protein kinase C zeta-inter-acting protein
    • Kuroda S, Nakagawa N, Tokunaga C, Tatematsu K, Tanizawa K. Mammalian homologue of the Caenorhabditis elegans UNC-76 protein involved in axonal outgrowth is a protein kinase C zeta-inter-acting protein. J Cell Biol 1999;114:403-411.
    • (1999) J Cell Biol , vol.114 , pp. 403-411
    • Kuroda, S.1    Nakagawa, N.2    Tokunaga, C.3    Tatematsu, K.4    Tanizawa, K.5
  • 5
    • 11144245872 scopus 로고    scopus 로고
    • Functional regulation of FEZ1 by the U-box-type Ubiquitin ligase E4B contribuyes to neuritogenesis
    • Okumura F, Hatakeyama S, Matsumoto M, Kamura T, Nakayama K. Functional regulation of FEZ1 by the U-box-type Ubiquitin ligase E4B contribuyes to neuritogenesis. J Biol Chem 2004;279:53533-53543.
    • (2004) J Biol Chem , vol.279 , pp. 53533-53543
    • Okumura, F.1    Hatakeyama, S.2    Matsumoto, M.3    Kamura, T.4    Nakayama, K.5
  • 7
    • 33845665844 scopus 로고    scopus 로고
    • Fasciculation and elongation protein zeta-1 (FEZ1) participates in the polarization of hippocampal neuron by controlling the mitochondrial motility
    • Ikuta J, Maturana A, Fujita T, Okajima T, Tatematsu Kenji, Tani-zawa K, Kuroda S. Fasciculation and elongation protein zeta-1 (FEZ1) participates in the polarization of hippocampal neuron by controlling the mitochondrial motility. Biochem Biophys Res Com-mun 2007;353:127-132.
    • (2007) Biochem Biophys Res Com-mun , vol.353 , pp. 127-132
    • Ikuta, J.1    Maturana, A.2    Fujita, T.3    Okajima, T.4    Kenji, T.5    Tani-zawa, K.6    Kuroda, S.7
  • 8
    • 33845967100 scopus 로고    scopus 로고
    • Two binding partners cooperate to activate the molecular motor Kinesin-1
    • Blasius TL, Cai D, Jih GT, Toret CP, Verhey KJ. Two binding partners cooperate to activate the molecular motor Kinesin-1. J Cell Biol 2007;176:11-17.
    • (2007) J Cell Biol , vol.176 , pp. 11-17
    • Blasius, T.L.1    Cai, D.2    Jih, G.T.3    Toret, C.P.4    Verhey, K.J.5
  • 10
    • 33744524659 scopus 로고    scopus 로고
    • FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region
    • Assmann EM, Alborghetti MR, Camargo MER, Kobarg J. FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region. J Biol Chem 2006;281:9869-9881.
    • (2006) J Biol Chem , vol.281 , pp. 9869-9881
    • Assmann, E.M.1    Alborghetti, M.R.2    Camargo, M.E.R.3    Kobarg, J.4
  • 12
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A, Nakamuraa H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett 2006;580:2041-2045.
    • (2006) FEBS Lett , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamuraa, H.2
  • 13
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 2005;272:5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 14
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interactrion network of Saccharomyces cerevisiae?
    • Ekman D, Light S, Bjorklund AK, Elofsson A. What properties characterize the hub proteins of the protein-protein interactrion network of Saccharomyces cerevisiae? Genome Biol 2006,7:R45.
    • (2006) Genome Biol , vol.7
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 16
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztanyi Z, Chen J, Dunker AK, Simon I, Tompa P. Disorder and sequence repeats in hub proteins and their implications for network evolution. J Proteome Res 2006;5:2985-2995.
    • (2006) J Proteome Res , vol.5 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 17
    • 34447558571 scopus 로고    scopus 로고
    • Intrinsic disorder in yeast transcriptional regulatory network
    • Singh GP, Dash D, Intrinsic disorder in yeast transcriptional regulatory network. Proteins 2007;68:602-605.
    • (2007) Proteins , vol.68 , pp. 602-605
    • Singh, G.P.1    Dash, D.2
  • 18
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 2005;579:3346-3354.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 19
    • 0036777533 scopus 로고    scopus 로고
    • Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T
    • Uversky VN, Fink AL. Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology 2002;23:553-567.
    • (2002) Neurotoxicology , vol.23 , pp. 553-567
    • Uversky, V.N.1    Fink, A.L.2
  • 22
    • 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 Inf Ser 1997;8:110-124.
    • (1997) Genome Inf Ser , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 24
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under the physiological conditions?
    • Uversky VN, Gillespie JR, Fin AL. Why are natively unfolded proteins unstructured under the physiological conditions? Proteins: Struct Funct Genet 2000;42:415-427.
    • (2000) Proteins: Struct Funct Genet , vol.42 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fin, A.L.3
  • 29
    • 27944488680 scopus 로고    scopus 로고
    • Accurate prediction of protein disordered regions by mining protein structure data
    • Cheng J, Sweredoski M, Baldi P. Accurate prediction of protein disordered regions by mining protein structure data. Data Mining Knowl Discov 2005;11:213-222.
    • (2005) Data Mining Knowl Discov , vol.11 , pp. 213-222
    • Cheng, J.1    Sweredoski, M.2    Baldi, P.3
  • 30
    • 0042622240 scopus 로고    scopus 로고
    • Glob plot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ. Glob plot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 2003;31:3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 31
    • 24044538903 scopus 로고    scopus 로고
    • IU Pred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I. IU Pred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005;21:3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 32
    • 18744405418 scopus 로고    scopus 로고
    • Prediction of unfolded segments in a protein sequence based on amino acid composition
    • Coeytaux K, Poupon A. Prediction of unfolded segments in a protein sequence based on amino acid composition. Bioinformatics 2005;21:1891-1900.
    • (2005) Bioinformatics , vol.21 , pp. 1891-1900
    • Coeytaux, K.1    Poupon, A.2
  • 33
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 2005;21:3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 34
    • 33747868721 scopus 로고    scopus 로고
    • Spritz: A server for the prediction of intrinsically disordered regions in protein sequences using kernel machines
    • Vullo A, Bortolami O, Pollastri G, Tosatto S. Spritz: a server for the prediction of intrinsically disordered regions in protein sequences using kernel machines Nucleic Acids Res 2006;34:W164-W168.
    • (2006) Nucleic Acids Res , vol.34
    • Vullo, A.1    Bortolami, O.2    Pollastri, G.3    Tosatto, S.4
  • 39
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005;7:176-182.
    • (2005) Proteins , vol.7 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 40
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J. Predicting coiled coils from protein sequences. Science 1991;252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 41
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two and three-stranded coiled coils
    • Wolf E, Kim PS, Berger B. MultiCoil: a program for predicting two and three-stranded coiled coils. Protein Sci 1997;6:1179-1189.
    • (1997) Protein Sci , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 42
    • 10844264054 scopus 로고    scopus 로고
    • Cavalcanti LP, Torriani IL, Plivelic TS, Oliveira CLP, Kellermann G, Neuenschwander. Two new sealed sample cells for small angle X-ray scattering from macromolecules in solution and complex fluids using synchrotron radiation. R Rev Sci Inst 2004;75:4541-4546.
    • Cavalcanti LP, Torriani IL, Plivelic TS, Oliveira CLP, Kellermann G, Neuenschwander. Two new sealed sample cells for small angle X-ray scattering from macromolecules in solution and complex fluids using synchrotron radiation. R Rev Sci Inst 2004;75:4541-4546.
  • 44
    • 60349106233 scopus 로고    scopus 로고
    • Guinier A, Fournet G. Small angle scattering of X-rays, translated by Walker CB and Yudowitch KL. New York: Wiley; 1955, pp 5-78.
    • Guinier A, Fournet G. Small angle scattering of X-rays, translated by Walker CB and Yudowitch KL. New York: Wiley; 1955, pp 5-78.
  • 47
    • 0002556772 scopus 로고
    • Glatter O, Kratky O, editors. London, New York: Academic Press;
    • Kirste RG, Oberthür RC. Small angle X-ray scattering. In: Glatter O, Kratky O, editors. London, New York: Academic Press; 1982, pp 387-431.
    • (1982) Small angle X-ray scattering , pp. 387-431
    • Kirste, R.G.1    Oberthür, R.C.2
  • 48
    • 33644606089 scopus 로고
    • Molecular-weight determination by light scattering
    • Debye PJ. Molecular-weight determination by light scattering. Phys Colloid Chem 1947;51:18-32.
    • (1947) Phys Colloid Chem , vol.51 , pp. 18-32
    • Debye, P.J.1
  • 50
    • 0034966446 scopus 로고    scopus 로고
    • Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering
    • Perez J, Vachette P, Russo D, Desmadril M, Durand D. Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering. J Mol Biol 2001;308:721-743.
    • (2001) J Mol Biol , vol.308 , pp. 721-743
    • Perez, J.1    Vachette, P.2    Russo, D.3    Desmadril, M.4    Durand, D.5
  • 51
    • 10044296373 scopus 로고    scopus 로고
    • SAXS study of the PIR domain from the Grb14 molecular adaptor: A natively unfolded protein with a transient structure primer?
    • Moncoq K, Broutin I, Craescu CT, Vachette P, Ducruix A, Durand D. SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? Biophys J 2004;87:4056-4064.
    • (2004) Biophys J , vol.87 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 52
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 1992;25:495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 53
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macro-molecules from solution scattering using simulated annealing
    • Svergun DI. Restoring low resolution structure of biological macro-molecules from solution scattering using simulated annealing. Biophys J 1999;76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 54
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI. Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 2003;36:860-864.
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 55
    • 0037031842 scopus 로고    scopus 로고
    • The Saccha-romyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. The Saccha-romyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J Biol Chem 2002;36:33447-33455.
    • (2002) J Biol Chem , vol.36 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 56
    • 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
  • 57
    • 33750472727 scopus 로고    scopus 로고
    • Characterization of the interaction between peptides derived from the gp120/V3 domain of HIV-1 and the amino terminal of the chemokine receptor CCR5 by NMR spectroscopy and light scattering
    • Rizos AK, Tsikalas I, Morikis D, Galanakis P, Spyroulias GA, Kram-bovitis E. Characterization of the interaction between peptides derived from the gp120/V3 domain of HIV-1 and the amino terminal of the chemokine receptor CCR5 by NMR spectroscopy and light scattering. J Non-Cryst Solids 2006;352:4451-4458.
    • (2006) J Non-Cryst Solids , vol.352 , pp. 4451-4458
    • Rizos, A.K.1    Tsikalas, I.2    Morikis, D.3    Galanakis, P.4    Spyroulias, G.A.5    Kram-bovitis, E.6
  • 61
    • 18244397937 scopus 로고    scopus 로고
    • Overexpression of fas-ciculation and elongation protein ζ-1 (FEZ1) induces a post-entry block to retroviruses in cultured cells
    • Naghavi MH, Hatziioannou T, Gao G, Goff SP. Overexpression of fas-ciculation and elongation protein ζ-1 (FEZ1) induces a post-entry block to retroviruses in cultured cells. Genes Dev 2005;19:1105-1115.
    • (2005) Genes Dev , vol.19 , pp. 1105-1115
    • Naghavi, M.H.1    Hatziioannou, T.2    Gao, G.3    Goff, S.P.4
  • 63
    • 0032549628 scopus 로고    scopus 로고
    • Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide
    • Shimizu K, Shirataki H, Honda T, Minami S, Takai Y. Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide. J Biol Chem 1998;273:6591-6594.
    • (1998) J Biol Chem , vol.273 , pp. 6591-6594
    • Shimizu, K.1    Shirataki, H.2    Honda, T.3    Minami, S.4    Takai, Y.5
  • 64
    • 10044261828 scopus 로고    scopus 로고
    • Natively unfolded domains in endo-cytosis: Hooks, lines and linkers
    • 5:1046-1052
    • Dafforn TR, Smith CJI. Natively unfolded domains in endo-cytosis: hooks, lines and linkers. EMBO reports 2004;5:1046-1052.
    • EMBO reports 2004
    • Dafforn, T.R.1    Smith, C.J.I.2
  • 65
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J Mol Biol 2004;337:635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 66
    • 44749086091 scopus 로고    scopus 로고
    • Lanza DCF, Trindade DM, Assmann EM, Kobarg J. Over-expression of GFP-FEZ1 causes generation of multi-lobulated nuclei mediated by microtubules in HEK293 cells. Exp Cell Res 2008, doi: 10.1016/j.yexcr, 2008.02.012
    • Lanza DCF, Trindade DM, Assmann EM, Kobarg J. Over-expression of GFP-FEZ1 causes generation of multi-lobulated nuclei mediated by microtubules in HEK293 cells. Exp Cell Res 2008, doi: 10.1016/j.yexcr, 2008.02.012


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