메뉴 건너뛰기




Volumn 11, Issue 4, 1998, Pages 183-191

Oligomerization of profilins from birch, man and yeast. Profilin, a ligand for itself?

Author keywords

Cytoskeleton; Oligomerization; Pollen; Profilin; Type I allergy

Indexed keywords

BETULA VERRUCOSA; ESCHERICHIA COLI; HOMO SAPIENS; SCHIZOSACCHAROMYCES POMBE;

EID: 0031729642     PISSN: 09340882     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004970050140     Document Type: Article
Times cited : (19)

References (56)
  • 1
    • 0028316191 scopus 로고
    • Purification, characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli
    • Almo SC, Pollard TD, Way M, Lattman, EE (1994) Purification, characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli. J Mol Biol 236:950-952
    • (1994) J Mol Biol , vol.236 , pp. 950-952
    • Almo, S.C.1    Pollard, T.D.2    Way, M.3    Lattman, E.E.4
  • 2
    • 0028153875 scopus 로고
    • Elucidation of the poly-L-proline binding site in Acanthamoeba profilin 1 by NRM spectroscopy
    • Archer SJ, Vinson VK, Pollard TD, Torchia DA (1994) Elucidation of the poly-L-proline binding site in Acanthamoeba profilin 1 by NRM spectroscopy. FEBS Lett 337:145-151
    • (1994) FEBS Lett , vol.337 , pp. 145-151
    • Archer, S.J.1    Vinson, V.K.2    Pollard, T.D.3    Torchia, D.A.4
  • 3
    • 0024500198 scopus 로고
    • Primary structure of human proacrosin deduced from its cDNA sequence
    • Baba T, Watanabe K, Kashiwabara S, Arai Y (1989) Primary structure of human proacrosin deduced from its cDNA sequence. FEBS Lett 244:296-300
    • (1989) FEBS Lett , vol.244 , pp. 296-300
    • Baba, T.1    Watanabe, K.2    Kashiwabara, S.3    Arai, Y.4
  • 5
    • 0027376752 scopus 로고
    • Mutagenesis of human profilin locates its poly-L-proline binding site to a hydrophobic patch of aromatic residues
    • Björkegren C, Rozycki M, Schutt CE, Lindberg U, Karlsson R (1993) Mutagenesis of human profilin locates its poly-L-proline binding site to a hydrophobic patch of aromatic residues. FEBS Lett 133:123-126
    • (1993) FEBS Lett , vol.133 , pp. 123-126
    • Björkegren, C.1    Rozycki, M.2    Schutt, C.E.3    Lindberg, U.4    Karlsson, R.5
  • 6
    • 0026639307 scopus 로고
    • Distribution of profilin in fibroblasts correlates with the presence of highly dynamic actin filaments
    • Buss F, Temm-Grove C, Henning S, Jokusch B (1992) Distribution of profilin in fibroblasts correlates with the presence of highly dynamic actin filaments. Cell Motil Cytoskeleton 22: 51-61
    • (1992) Cell Motil Cytoskeleton , vol.22 , pp. 51-61
    • Buss, F.1    Temm-Grove, C.2    Henning, S.3    Jokusch, B.4
  • 7
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier MF, Pantaloni D (1997) Control of actin dynamics in cell motility. J Mol Biol 269:459-467
    • (1997) J Mol Biol , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 8
    • 0027163104 scopus 로고
    • Modulation of the interaction between G-actin and thymosin beta-4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics
    • Carlier MF, Jean C, Rieger KA, Lenfant M, Pantaloni D (1993) Modulation of the interaction between G-actin and thymosin beta-4 by the ATP/ADP ratio: possible implication in the regulation of actin dynamics. Proc Natl Acad Sci USA 90:5034-5038
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5034-5038
    • Carlier, M.F.1    Jean, C.2    Rieger, K.A.3    Lenfant, M.4    Pantaloni, D.5
  • 9
    • 0030958087 scopus 로고    scopus 로고
    • cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang F, Drubin D, Nurse P (1997) cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J Cell Biol 137:169-182
    • (1997) J Cell Biol , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 10
    • 0027935843 scopus 로고
    • Stability of yeast iso-l-ferricytochrome c as a function of pH and temperature
    • Cohen DS, Pielak GJ (1994) Stability of yeast iso-l-ferricytochrome c as a function of pH and temperature. Protein Sci 3:1253-1260
    • (1994) Protein Sci , vol.3 , pp. 1253-1260
    • Cohen, D.S.1    Pielak, G.J.2
  • 11
    • 0031567492 scopus 로고    scopus 로고
    • Birch pollen profilin: Structural organization and interaction with poly-L-proline peptides as revealed by NMR
    • Domke T, Federau T, Schlüter K, Giehl K, Valenta R, Schomburg D, Jockusch BM (1997) Birch pollen profilin: structural organization and interaction with poly-L-proline peptides as revealed by NMR. FEBS Lett 411:291-295
    • (1997) FEBS Lett , vol.411 , pp. 291-295
    • Domke, T.1    Federau, T.2    Schlüter, K.3    Giehl, K.4    Valenta, R.5    Schomburg, D.6    Jockusch, B.M.7
  • 12
    • 0028105664 scopus 로고
    • Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin
    • Drobak BK, Watkins PAC, Valenta R, Dove SK, Lloyd CW, Staiger CJ (1994) Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin. Plant J 6:389-400
    • (1994) Plant J , vol.6 , pp. 389-400
    • Drobak, B.K.1    Watkins, P.A.C.2    Valenta, R.3    Dove, S.K.4    Lloyd, C.W.5    Staiger, C.J.6
  • 13
    • 0017718187 scopus 로고
    • Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes
    • Elwell ML, Schellmann JA (1977) Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. Biochim Biophys Acta 494: 367-383
    • (1977) Biochim Biophys Acta , vol.494 , pp. 367-383
    • Elwell, M.L.1    Schellmann, J.A.2
  • 15
    • 0027968554 scopus 로고
    • Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli
    • Fedorov AA, Pollard TD, Almo SC (1994) Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli. J Mol Biol 241:480-482
    • (1994) J Mol Biol , vol.241 , pp. 480-482
    • Fedorov, A.A.1    Pollard, T.D.2    Almo, S.C.3
  • 16
    • 0031568307 scopus 로고    scopus 로고
    • The molecular basis for allergen cross-reactivity: Crystal structure and IgE-epitope mapping of birch pollen profilin
    • Fedorov AA, Ball T, Mahoney NM, Valenta R, Almo SC (1997) The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin. Structure 5:33-45
    • (1997) Structure , vol.5 , pp. 33-45
    • Fedorov, A.A.1    Ball, T.2    Mahoney, N.M.3    Valenta, R.4    Almo, S.C.5
  • 17
    • 0031022598 scopus 로고    scopus 로고
    • Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c
    • Fetrow JS, Horner SR, Öhrl W, Schaak DL, Boose TL, Burton RE (1997) Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c. Protein Sci 6:195-208
    • (1997) Protein Sci , vol.6 , pp. 195-208
    • Fetrow, J.S.1    Horner, S.R.2    Öhrl, W.3    Schaak, D.L.4    Boose, T.L.5    Burton, R.E.6
  • 18
    • 0022539027 scopus 로고
    • Peptid and protein molecular weight determination by electrophoresis using a high-molarity Tris buffer system without urea
    • Fling SP, Gregerson DS (1986) Peptid and protein molecular weight determination by electrophoresis using a high-molarity Tris buffer system without urea. Analyt Biochem 155:83-88
    • (1986) Analyt Biochem , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 19
    • 0031194074 scopus 로고    scopus 로고
    • Actin cytoskeleton: Are FH proteins local organizers?
    • Frazier JA, Field CM (1997) Actin cytoskeleton: are FH proteins local organizers? Curr Biol 7:414-417
    • (1997) Curr Biol , vol.7 , pp. 414-417
    • Frazier, J.A.1    Field, C.M.2
  • 22
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta-4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, Safer D, Nachmias VT, Pollard TD (1992) The control of actin nucleotide exchange by thymosin beta-4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell 3:1015-1024
    • (1992) Mol Biol Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 23
    • 0029158828 scopus 로고
    • Localization of profilin- and actin-like immunoreactivity in in vitro-germinated tobacco pollen tubes by electron microscopy after special water-free fixation techniques
    • Grote M, Swoboda I, Meagher RB, Valenta R (1995) Localization of profilin- and actin-like immunoreactivity in in vitro-germinated tobacco pollen tubes by electron microscopy after special water-free fixation techniques. Sex Plant Reprod 8:180-186
    • (1995) Sex Plant Reprod , vol.8 , pp. 180-186
    • Grote, M.1    Swoboda, I.2    Meagher, R.B.3    Valenta, R.4
  • 24
    • 0030771772 scopus 로고    scopus 로고
    • Profilin revealed in pollen nuclei: Immuno-electron microscopy of high-pressure frozen Ledebouria socialis Roth (Hyacinthaceae)
    • Hess MW, Valenta R (1997) Profilin revealed in pollen nuclei: immuno-electron microscopy of high-pressure frozen Ledebouria socialis Roth (Hyacinthaceae). Sex Plant Reprod 10:283-287
    • (1997) Sex Plant Reprod , vol.10 , pp. 283-287
    • Hess, M.W.1    Valenta, R.2
  • 25
    • 0030666511 scopus 로고    scopus 로고
    • Microinjection of profilins from different sources into the green alga Micrasterias causes transient inhibition of cell growth
    • Holzinger A, Mittermann I, Laffer S, Valenta R, Meindl U (1997) Microinjection of profilins from different sources into the green alga Micrasterias causes transient inhibition of cell growth. Protoplasma 199:124-134
    • (1997) Protoplasma , vol.199 , pp. 124-134
    • Holzinger, A.1    Mittermann, I.2    Laffer, S.3    Valenta, R.4    Meindl, U.5
  • 26
    • 0030927327 scopus 로고    scopus 로고
    • Bnilp and Bnrlp: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura H, Tanaka K, Hihara T, Umikawa M, Kamei T, Takahashi K, Sasaki T, Takai Y (1997) Bnilp and Bnrlp: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J 16:2745-2755
    • (1997) EMBO J , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 27
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidyl-inositol-4,5-bisphosphate and profilactin
    • Lassing I, Lindberg U (1985) Specific interaction between phosphatidyl-inositol-4,5-bisphosphate and profilactin. Nature 1314: 472-474
    • (1985) Nature , vol.1314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 28
  • 29
    • 0024289542 scopus 로고
    • The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes
    • Lindberg U, Schutt CE, Hellsten E, Tjäder AC, Huit T (1988) The use of poly(L-proline)-Sepharose in the isolation of profilin and profilactin complexes. Biochem Biophys Acta 967:391-400
    • (1988) Biochem Biophys Acta , vol.967 , pp. 391-400
    • Lindberg, U.1    Schutt, C.E.2    Hellsten, E.3    Tjäder, A.C.4    Huit, T.5
  • 30
    • 0027358716 scopus 로고
    • Profilin as a potential mediator of membrane-cytoskeleton communication
    • Machesky LM, Pollard TD (1993) Profilin as a potential mediator of membrane-cytoskeleton communication. Trends Cell Biol 3:381-385
    • (1993) Trends Cell Biol , vol.3 , pp. 381-385
    • Machesky, L.M.1    Pollard, T.D.2
  • 31
    • 0025517560 scopus 로고
    • The affinities of human platelet and Acanthamoeba profilins accounts for their relative abilities to inhibit phospholipase C
    • Machesky LM, Goldschmidt-Clermont PJ, Pollard TD (1990) The affinities of human platelet and Acanthamoeba profilins accounts for their relative abilities to inhibit phospholipase C. Cell Regul 1:937-950
    • (1990) Cell Regul , vol.1 , pp. 937-950
    • Machesky, L.M.1    Goldschmidt-Clermont, P.J.2    Pollard, T.D.3
  • 32
    • 0028108647 scopus 로고
    • Identification of the poly-L-proline-binding site on human profilin
    • Metzler WJ, Bell AJ, Ernst E, Lavoie TB, Mueller L (1994) Identification of the poly-L-proline-binding site on human profilin. J Biol Chem 269:4620-4625
    • (1994) J Biol Chem , vol.269 , pp. 4620-4625
    • Metzler, W.J.1    Bell, A.J.2    Ernst, E.3    Lavoie, T.B.4    Mueller, L.5
  • 33
    • 0029152581 scopus 로고
    • Molecular cloning and characterization of profilin from tobacco (Nicotiana tabacum); increased profilin expression during pollen maturation
    • Mittermann I, Swoboda I, Pierson E, Eller N, Kraft D, Valenta R, Heberle-Bors E (1995) Molecular cloning and characterization of profilin from tobacco (Nicotiana tabacum); increased profilin expression during pollen maturation. Plant Mol Biol 27:137-146
    • (1995) Plant Mol Biol , vol.27 , pp. 137-146
    • Mittermann, I.1    Swoboda, I.2    Pierson, E.3    Eller, N.4    Kraft, D.5    Valenta, R.6    Heberle-Bors, E.7
  • 34
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mockrin SC, Korn ED (1980) Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19:5359-5362
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 35
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta-4
    • Pantaloni D, Carlier MF (1993) How profilin promotes actin filament assembly in the presence of thymosin beta-4. Cell 75:1007-1014
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 36
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA (1986) Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem 55:987-1035
    • (1986) Annu Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 38
    • 9044250098 scopus 로고    scopus 로고
    • Plant and animal profilins are functionally equivalent and stabilize microfilaments in living animal cells
    • Rothkegel M, Mayboroda O, Rohde M, Wucherpfennig C, Valenta R, Jokusch BM (1996) Plant and animal profilins are functionally equivalent and stabilize microfilaments in living animal cells. J Cell Sci 109:83-90
    • (1996) J Cell Sci , vol.109 , pp. 83-90
    • Rothkegel, M.1    Mayboroda, O.2    Rohde, M.3    Wucherpfennig, C.4    Valenta, R.5    Jokusch, B.M.6
  • 41
    • 0028464361 scopus 로고
    • Profilin: At the crossroads of signal transduction and the actin cytoskeleton
    • Sohn RH, Goldschmidt-Clermont PJ (1994) Profilin: at the crossroads of signal transduction and the actin cytoskeleton. Bioessays 16:465-472
    • (1994) Bioessays , vol.16 , pp. 465-472
    • Sohn, R.H.1    Goldschmidt-Clermont, P.J.2
  • 42
    • 0028385716 scopus 로고
    • Microinjected plant profilin affects cytoplasmic streaming by rapidly depolymerizing F-actin
    • Staiger CJ, Yuan M, Valenta R, Shaw P, Warn R, Lloyd CW (1994) Microinjected plant profilin affects cytoplasmic streaming by rapidly depolymerizing F-actin. Curr Biol 4:215-219
    • (1994) Curr Biol , vol.4 , pp. 215-219
    • Staiger, C.J.1    Yuan, M.2    Valenta, R.3    Shaw, P.4    Warn, R.5    Lloyd, C.W.6
  • 43
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland EH (1974) Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem 2:113-174
    • (1974) CRC Crit Rev Biochem , vol.2 , pp. 113-174
    • Strickland, E.H.1
  • 45
    • 0022409564 scopus 로고
    • Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin
    • Tanaka M, Shibata H (1985) Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin. Eur J Biochem 151:291-297
    • (1985) Eur J Biochem , vol.151 , pp. 291-297
    • Tanaka, M.1    Shibata, H.2
  • 46
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts
    • Theriot JA, Rosenblatt J, Portnoy DA, Goldschmidt-Clermont PJ, Mitchison TJ (1994) Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell 76:505-517
    • (1994) Cell , vol.76 , pp. 505-517
    • Theriot, J.A.1    Rosenblatt, J.2    Portnoy, D.A.3    Goldschmidt-Clermont, P.J.4    Mitchison, T.J.5
  • 48
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 52
    • 0026786298 scopus 로고
    • Purification and characterization of an allergen from celery immunchemically related to an allergen present in several other plant species. Identification as a profilin
    • Vallier P, Dechamp C, Valenta R, Vial O, Deviller P (1992) Purification and characterization of an allergen from celery immunchemically related to an allergen present in several other plant species. Identification as a profilin. Clin Exp Allergy 22:774-782
    • (1992) Clin Exp Allergy , vol.22 , pp. 774-782
    • Vallier, P.1    Dechamp, C.2    Valenta, R.3    Vial, O.4    Deviller, P.5
  • 53
    • 0031432209 scopus 로고    scopus 로고
    • Probing the plant actin cytoskeleton during cytokinesis and interphase by profilin microinjection
    • Valster AH, Pierson ES, Valenta R, Hepler PK, Emons AMC (1997) Probing the plant actin cytoskeleton during cytokinesis and interphase by profilin microinjection. Plant Cell 9:1815-1824
    • (1997) Plant Cell , vol.9 , pp. 1815-1824
    • Valster, A.H.1    Pierson, E.S.2    Valenta, R.3    Hepler, P.K.4    Emons, A.M.C.5
  • 54
    • 0030909875 scopus 로고    scopus 로고
    • Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum
    • Vidali L, Hepler PK (1997) Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum. Cell Motil Cytoskel 36:323-338
    • (1997) Cell Motil Cytoskel , vol.36 , pp. 323-338
    • Vidali, L.1    Hepler, P.K.2
  • 55
    • 0029910404 scopus 로고    scopus 로고
    • Induction of IgE antibodies in mice and rhesus monkeys with recombinant birch pollen allergens: Different allergenicity of Bet v 1 and Bet v 2
    • Vrtala S, Mayer P, Ferreira F, Susani M, Sehon AH, Kraft D, Valenta R (1996) Induction of IgE antibodies in mice and rhesus monkeys with recombinant birch pollen allergens: different allergenicity of Bet v 1 and Bet v 2. J Allergy Clin Immunol 98:913-921
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 913-921
    • Vrtala, S.1    Mayer, P.2    Ferreira, F.3    Susani, M.4    Sehon, A.H.5    Kraft, D.6    Valenta, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.