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Volumn 6, Issue 9, 2007, Pages 3648-3654

Fesselin is a natively unfolded protein

Author keywords

Circular dichroism; Fesselin; Fluorescence quenching; Natively unfolded; PONDR

Indexed keywords

ACTIN BINDING PROTEIN; CAD PROTEIN; CALMODULIN BINDING PROTEIN; PROTEIN CAD22; PROTEIN FESSELIN; SYNAPTOPODIN; SYNAPTOPODIN 2; UNCLASSIFIED DRUG;

EID: 34948830161     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr070237v     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 34948895676 scopus 로고    scopus 로고
    • The actin nucleating protein, Fesselin, is a member of the synaptopodin family
    • Suppl. Abstract
    • Schroeter, M.; Beall, B.; Heid, H.; Chalovich, J. M. The actin nucleating protein, Fesselin, is a member of the synaptopodin family. Biophys. J. Suppl. Abstract, 2006, 578.
    • (2006) Biophys. J , pp. 578
    • Schroeter, M.1    Beall, B.2    Heid, H.3    Chalovich, J.M.4
  • 2
    • 0038860948 scopus 로고
    • Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin
    • Sobue, K.; Muramoto, Y.; Fujita, M.; Kakiuchi, S. Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 5652-5655.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 5652-5655
    • Sobue, K.1    Muramoto, Y.2    Fujita, M.3    Kakiuchi, S.4
  • 3
    • 0022930623 scopus 로고
    • Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle
    • Takahashi, K.; Hiwada, K.; Kokubu, T. Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle. Biochem. Biophys. Res. Commun. 1986, 141, 20-26.
    • (1986) Biochem. Biophys. Res. Commun , vol.141 , pp. 20-26
    • Takahashi, K.1    Hiwada, K.2    Kokubu, T.3
  • 4
    • 0032856424 scopus 로고    scopus 로고
    • Leinweber, B. D.; Fredricksen, R. S.; Hoffman, D. R.; Chalovich, J. M. Fesselin: a novel synaptopodin-like actin binding protein from muscle tissue. J. Muscle Res. Cell. Motil. 1999, 20, 539-545.
    • Leinweber, B. D.; Fredricksen, R. S.; Hoffman, D. R.; Chalovich, J. M. Fesselin: a novel synaptopodin-like actin binding protein from muscle tissue. J. Muscle Res. Cell. Motil. 1999, 20, 539-545.
  • 5
    • 0035851920 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
    • Weins, A.; Schwarz, K.; Faul, C.; Barisoni, L.; Linke, W. A.; Mundel, P. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J. Cell Biol. 2001, 155, 393-404.
    • (2001) J. Cell Biol , vol.155 , pp. 393-404
    • Weins, A.1    Schwarz, K.2    Faul, C.3    Barisoni, L.4    Linke, W.A.5    Mundel, P.6
  • 6
    • 0035960656 scopus 로고    scopus 로고
    • Beall, B.; Chalovich, J. M. Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization. Biochemistry 2001, 40, 14252-14259.
    • Beall, B.; Chalovich, J. M. Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization. Biochemistry 2001, 40, 14252-14259.
  • 7
    • 7244245361 scopus 로고    scopus 로고
    • 2+-calmodulin regulates fesselin-induced actin polymerization
    • 2+-calmodulin regulates fesselin-induced actin polymerization. Biochemistry 2004, 43, 13875-13882.
    • (2004) Biochemistry , vol.43 , pp. 13875-13882
    • Schroeter, M.1    Chalovich, J.M.2
  • 8
    • 28444478088 scopus 로고    scopus 로고
    • Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity
    • Schroeter, M. M.; Chalovich, J. M. Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity. J. Muscle Res. Cell. Motil. 2005, 26, 183-189.
    • (2005) J. Muscle Res. Cell. Motil , vol.26 , pp. 183-189
    • Schroeter, M.M.1    Chalovich, J.M.2
  • 9
    • 33746053239 scopus 로고    scopus 로고
    • Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity towards actin polymerization
    • Pham, M.; Chalovich, J. M. Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity towards actin polymerization. J. Muscle Res. Cell. Motil. 2006, 27, 45-51.
    • (2006) J. Muscle Res. Cell. Motil , vol.27 , pp. 45-51
    • Pham, M.1    Chalovich, J.M.2
  • 10
    • 4644363346 scopus 로고    scopus 로고
    • Fesselin is a target protein for calmodulin in a calcium-dependent manner
    • Kolakowski, J.; Wrzosek, A.; Dabrowska, R. Fesselin is a target protein for calmodulin in a calcium-dependent manner. Biochem. Biophys. Res. Commun. 2004, 323, 1251-1256.
    • (2004) Biochem. Biophys. Res. Commun , vol.323 , pp. 1251-1256
    • Kolakowski, J.1    Wrzosek, A.2    Dabrowska, R.3
  • 11
    • 34948838466 scopus 로고    scopus 로고
    • Localization of the actin-binding protein fesselin in chicken smooth muscle
    • Suppl. Abstract
    • Schroeter, M.; Renegar, R. H.; Leinweber, B. D.; Zary, J. T.; Chalovich, J. M. Localization of the actin-binding protein fesselin in chicken smooth muscle. Biophys. J. Suppl. Abstract, 2007, 815.
    • (2007) Biophys. J , pp. 815
    • Schroeter, M.1    Renegar, R.H.2    Leinweber, B.D.3    Zary, J.T.4    Chalovich, J.M.5
  • 12
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright, P. E.; Dyson, H. J. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293, 321-331.
    • (1999) J. Mol. Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 13
    • 0028170411 scopus 로고
    • Structural studies of Tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
    • Schweers, O.; Schonbrunn-Hanebeck, E.; Marx, A.; Mandelkow, E. Structural studies of Tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J. Biol. Chem. 1994, 269, 24920.
    • (1994) J. Biol. Chem , vol.269 , pp. 24920
    • Schweers, O.1    Schonbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 15
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. 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
  • 16
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded
    • Uversky, V. N. 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
  • 17
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter, M.; Tompa, P.; Simon, I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics 2007, 23, 950-956.
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 18
    • 0344980717 scopus 로고    scopus 로고
    • Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin
    • Permyakov, S. E.; Millett, I. S.; Doniach, S.; Permyakov, E. A.; Uversky, V. N. Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins 2003, 53, 855-862.
    • (2003) Proteins , vol.53 , pp. 855-862
    • Permyakov, S.E.1    Millett, I.S.2    Doniach, S.3    Permyakov, E.A.4    Uversky, V.N.5
  • 19
    • 0028831760 scopus 로고
    • Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs
    • Schenk, P. M.; Baumann, S.; Mattes, R.; Steinbiss, H. H. Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs. BioTechniques 1995, 19, 200, 196-198.
    • (1995) BioTechniques , vol.19 , Issue.200 , pp. 196-198
    • Schenk, P.M.1    Baumann, S.2    Mattes, R.3    Steinbiss, H.H.4
  • 20
    • 0038182972 scopus 로고    scopus 로고
    • Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site
    • Fredricksen, S.; Cai, A.; Gafurov, B.; Resetar, A.; Chalovich, J. M. Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site. Biochemistry 2003, 42, 6136-6148.
    • (2003) Biochemistry , vol.42 , pp. 6136-6148
    • Fredricksen, S.1    Cai, A.2    Gafurov, B.3    Resetar, A.4    Chalovich, J.M.5
  • 22
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G.; Taylor, R. S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 1975, 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 23
    • 0020983480 scopus 로고
    • Purification of plant calmodulin
    • Anderson, J. M. Purification of plant calmodulin. Methods Enzymol. 1983, 102, 9-17.
    • (1983) Methods Enzymol , vol.102 , pp. 9-17
    • Anderson, J.M.1
  • 25
    • 0042622240 scopus 로고    scopus 로고
    • Linding, R.; Russell, R. B.; Neduva, V.; Gibson, T. J. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 2003, 31, 3701-3708.
    • Linding, R.; Russell, R. B.; Neduva, V.; Gibson, T. J. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 2003, 31, 3701-3708.
  • 26
    • 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
  • 27
    • 33646919599 scopus 로고    scopus 로고
    • Prediction of natively unfolded regions in protein chain
    • Galzitskaya, O. V.; Garbuzynskiy, S. O.; Lobanov, M. Y. Prediction of natively unfolded regions in protein chain. Mol. Biol. 2006, 40, 298-304.
    • (2006) Mol. Biol , vol.40 , pp. 298-304
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 29
    • 0034669882 scopus 로고    scopus 로고
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are natively unfolded proteins unstructured under physiologic conditions. Proteins 2000, 41, 415-427.
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are "natively unfolded" proteins unstructured under physiologic conditions. Proteins 2000, 41, 415-427.
  • 30
    • 0035882542 scopus 로고    scopus 로고
    • Denatured collapsed states in protein folding: Example of apomyoglobin
    • Tcherkasskaya, O.; Uversky, V. N. Denatured collapsed states in protein folding: example of apomyoglobin. Proteins 2001, 44, 244-254.
    • (2001) Proteins , vol.44 , pp. 244-254
    • Tcherkasskaya, O.1    Uversky, V.N.2
  • 32
    • 0038860948 scopus 로고
    • Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin
    • Sobue, K.; Muramoto, Y.; Fujita, M.; Kakiuchi, S. Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 5652.
    • (1981) Proc. Natl. Acad. Sci. U.S.A , vol.78 , pp. 5652
    • Sobue, K.1    Muramoto, Y.2    Fujita, M.3    Kakiuchi, S.4
  • 33
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler, A. J.; Greenfield, N. J.; Fasman, G. D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 1973, 27, 675-735.
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 34
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A. L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 2005, 15, 35-41.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 36
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M.; Simon, I.; Friedrich, P.; Tompa, P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 2004, 338, 1015-1026.
    • (2004) J. Mol. Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 37
    • 24944546549 scopus 로고    scopus 로고
    • Coupled binding and folding with α-helix-forming Molecular Recognition Elements
    • Oldfield, C. J.; Cheng, Y.; Cortese, M. S.; Romero, P.; Uversky, V. N.; Dunker, K. A. Coupled binding and folding with α-helix-forming Molecular Recognition Elements. Biochemistry 2005, 44, 12454-12470.
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, K.A.6
  • 39
    • 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
  • 40
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis, J.-M.; Johansson, K.; Receveur-Brechot, V.; Oldfield, C. J.; Dunker, K. A.; Canard, B.; Longhi, S. The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res. 2004, 99, 157-167.
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.-M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5    Canard, B.6    Longhi, S.7
  • 41
    • 33846317372 scopus 로고    scopus 로고
    • Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins
    • Ng, K. P.; Potikyan, G.; Savene, R. O. V.; Denny, C. T.; Uversky, V. N.; Lee, K. A. W. Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 479-484.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 479-484
    • Ng, K.P.1    Potikyan, G.2    Savene, R.O.V.3    Denny, C.T.4    Uversky, V.N.5    Lee, K.A.W.6
  • 42
    • 0027146350 scopus 로고
    • Conformation of thymosin beta 4 in water determined by NMR spectroscopy
    • Czisch, M.; Schleicher, M.; Horger, S.; Voelter, W.; Holak, T. A. Conformation of thymosin beta 4 in water determined by NMR spectroscopy. Eur. J. Biochem. 1993, 218, 335-344.
    • (1993) Eur. J. Biochem , vol.218 , pp. 335-344
    • Czisch, M.1    Schleicher, M.2    Horger, S.3    Voelter, W.4    Holak, T.A.5
  • 43
    • 0034624753 scopus 로고    scopus 로고
    • Kim, A. S.; Kakalis, L. T.; Abdul-Manan, N.; Liu, G. A.; Rosen, M. K Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 2000, 404, 151-158.
    • Kim, A. S.; Kakalis, L. T.; Abdul-Manan, N.; Liu, G. A.; Rosen, M. K Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 2000, 404, 151-158.
  • 44
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J.; Sodhi, J. S.; McGuffin, L. J.; Buxton, B. F.; Jones, D. T. 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
  • 45
    • 33847768609 scopus 로고    scopus 로고
    • Functional antology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • Xie, H.; Vucetic, S.; Iakoucheva, L. M.; Oldfield, C. J.; Dunker, K. A.; Uversky, V. N.; Obradovic, Z. Functional antology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J. Proteome Res. 2007, 6, 1882-1898.
    • (2007) J. Proteome Res , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, K.A.5    Uversky, V.N.6    Obradovic, Z.7


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