메뉴 건너뛰기




Volumn 3, Issue , 2002, Pages 1-8

Hisactophilin is involved in osmoprotection in Dictyostelium

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CYTOSKELETON PROTEIN; HISACTOPHILIN; HYPERTONIC SOLUTION; MUTANT PROTEIN; PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 3343012103     PISSN: 14712091     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2091-3-10     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0029118574 scopus 로고
    • Cell volume regulated transporters of compatible osmolytes
    • Kwon HM, Handler JS: Cell volume regulated transporters of compatible osmolytes. Curr. Opin. Cell Biol. 1995, 7:465-471
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 465-471
    • Kwon, H.M.1    Handler, J.S.2
  • 2
    • 0029395010 scopus 로고
    • Stress signaling in yeast
    • Ruis H, Schüller C: Stress signaling in yeast. BioEssays 1995, 17:959-965
    • (1995) BioEssays , vol.17 , pp. 959-965
    • Ruis, H.1    Schüller, C.2
  • 3
    • 0025946371 scopus 로고
    • Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells
    • Cohen D, Wassermann J, Gullans S: Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells. Am. J. Physiol. 1991, 261:C594-C601
    • (1991) Am. J. Physiol. , vol.261
    • Cohen, D.1    Wassermann, J.2    Gullans, S.3
  • 4
    • 0026534772 scopus 로고
    • Hypertonic stress induces alpha B-crystallin expression
    • Dasgupta S, Hohmann TC, Carper D: Hypertonic stress induces alpha B-crystallin expression. Exp. Eye Res. 1992, 54:461-470
    • (1992) Exp. Eye Res. , vol.54 , pp. 461-470
    • Dasgupta, S.1    Hohmann, T.C.2    Carper, D.3
  • 5
    • 0033517111 scopus 로고    scopus 로고
    • Rearrangement of cortex proteins constitutes an osmoprotective mechanism in Dictyostelium
    • Zischka H, Oehme F, Pintsch T, Ott A, Keller H, Kellermann J, Schuster SC: Rearrangement of cortex proteins constitutes an osmoprotective mechanism in Dictyostelium. EMBO J. 1999, 18:4241-4249
    • (1999) EMBO J. , vol.18 , pp. 4241-4249
    • Zischka, H.1    Oehme, F.2    Pintsch, T.3    Ott, A.4    Keller, H.5    Kellermann, J.6    Schuster, S.C.7
  • 6
    • 0030024280 scopus 로고    scopus 로고
    • Protection against osmotic stress by cGMP-mediated myosin phosphorylation
    • Kuwayama H, Ecke M, Gerisch G, Van Haastert PJ: Protection against osmotic stress by cGMP-mediated myosin phosphorylation. Science 1996, 271:207-209
    • (1996) Science , vol.271 , pp. 207-209
    • Kuwayama, H.1    Ecke, M.2    Gerisch, G.3    Van Haastert, P.J.4
  • 7
    • 0030134626 scopus 로고    scopus 로고
    • The big squeeze. Osmoregulation
    • Insall RH: Cyclic GMP and the big squeeze. Osmoregulation. Curr. Biol. 1996, 6:516-518
    • (1996) Curr. Biol. , vol.6 , pp. 516-518
    • Insall, R.H.1    Cyclic, G.M.P.2
  • 8
    • 0031917737 scopus 로고    scopus 로고
    • DdLIM is a cytoskeleton-associated protein involved in the protrusion of lamellipodia in Dictyostelium
    • Prassler J, Murr A, Stocker S, Faix J, Murphy J, Marriott G: DdLIM is a cytoskeleton-associated protein involved in the protrusion of lamellipodia in Dictyostelium. Mol. Biol. Cell 1998, 9:545-559
    • (1998) Mol. Biol. Cell , vol.9 , pp. 545-559
    • Prassler, J.1    Murr, A.2    Stocker, S.3    Faix, J.4    Murphy, J.5    Marriott, G.6
  • 9
    • 85029461869 scopus 로고    scopus 로고
    • Ph.D. Thesis., Ludwig-Maximilians-University, Munich
    • Oehme F: Ph.D. Thesis., Ludwig-Maximilians-University, Munich. 1999
    • (1999)
    • Oehme, F.1
  • 10
    • 0031729828 scopus 로고    scopus 로고
    • High levels of actin tyrosine phosphorylation: Correlation with the dormant state of Dictyostelium spores
    • Kishi Y, Clements C, Mahadeo DC, Cotter DA, Sameshima M: High levels of actin tyrosine phosphorylation: correlation with the dormant state of Dictyostelium spores. J. Cell Sci. 1998, 111:2923-2932
    • (1998) J. Cell Sci. , vol.111 , pp. 2923-2932
    • Kishi, Y.1    Clements, C.2    Mahadeo, D.C.3    Cotter, D.A.4    Sameshima, M.5
  • 11
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • Rivero F, Koppel B, Peracino B, Bozzaro S, Siegert F, Weijer CJ, Schleicher M, Albrecht R, Noegel AA: The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J. Cell Sci. 1996, 109:2679-2691
    • (1996) J. Cell Sci. , vol.109 , pp. 2679-2691
    • Rivero, F.1    Koppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Weijer, C.J.6    Schleicher, M.7    Albrecht, R.8    Noegel, A.A.9
  • 12
    • 13344276590 scopus 로고    scopus 로고
    • cGMP accumulation induced by hypertonic stress in Dictyostelium discoideum
    • Oyama M: cGMP accumulation induced by hypertonic stress in Dictyostelium discoideum. J. Biol. Chem. 1996, 271:5574-5579
    • (1996) J. Biol. Chem. , vol.271 , pp. 5574-5579
    • Oyama, M.1
  • 13
    • 0027372314 scopus 로고
    • Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo
    • Egelhoff TT, Lee RJ, Spudich JA: Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo. Cell 1993, 75:363-371
    • (1993) Cell , vol.75 , pp. 363-371
    • Egelhoff, T.T.1    Lee, R.J.2    Spudich, J.A.3
  • 14
    • 0029783214 scopus 로고    scopus 로고
    • The hybrid histidine kinase DokA is part of the osmotic response system of Dictyostelium
    • Schuster SC, Noegel AA, Oehme F, Gerisch G, Simon MI.: The hybrid histidine kinase DokA is part of the osmotic response system of Dictyostelium. EMBO J. 1996, 15:3880-3889
    • (1996) EMBO J. , vol.15 , pp. 3880-3889
    • Schuster, S.C.1    Noegel, A.A.2    Oehme, F.3    Gerisch, G.4    Simon, M.I.5
  • 15
    • 0034329385 scopus 로고    scopus 로고
    • Osmotic stress response in Dictyostelium is mediated by cAMP
    • Ott A, Oehme F, Keller H, Schuster SC: Osmotic stress response in Dictyostelium is mediated by cAMP. EMBO J. 2000, 19:5782-5792
    • (2000) EMBO J. , vol.19 , pp. 5782-5792
    • Ott, A.1    Oehme, F.2    Keller, H.3    Schuster, S.C.4
  • 16
    • 0027476154 scopus 로고
    • The integral membrane protein, ponticulin, acts as a monomer in nucleating actin assembly
    • Chia C, Shariff A, Savage S, Luna E: The integral membrane protein, ponticulin, acts as a monomer in nucleating actin assembly. J. Cell Biol. 1993, 120:909-922
    • (1993) J. Cell Biol. , vol.120 , pp. 909-922
    • Chia, C.1    Shariff, A.2    Savage, S.3    Luna, E.4
  • 17
    • 0028936379 scopus 로고
    • The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm
    • Hanakam F, Eckerskorn C, Lottspeich F, Muller-Taubenberger A, Schafer W, Gerisch G: The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm. J. Biol. Chem. 1995, 270:596-602
    • (1995) J. Biol. Chem. , vol.270 , pp. 596-602
    • Hanakam, F.1    Eckerskorn, C.2    Lottspeich, F.3    Muller-Taubenberger, A.4    Schafer, W.5    Gerisch, G.6
  • 18
    • 0028822689 scopus 로고
    • The actin-binding protein hisactophilin binds in vitro to partially charged membranes and mediates actin coupling to membranes
    • Behrisch A, Dietrich C, Noegel AA, Schleicher M, Sackmann E: The actin-binding protein hisactophilin binds in vitro to partially charged membranes and mediates actin coupling to membranes. Biochemistry 1995, 34:15182-15190
    • (1995) Biochemistry , vol.34 , pp. 15182-15190
    • Behrisch, A.1    Dietrich, C.2    Noegel, A.A.3    Schleicher, M.4    Sackmann, E.5
  • 19
    • 0029760018 scopus 로고    scopus 로고
    • Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch
    • Hanakam F, Gerisch G, Lotz S, Alt T, Seelig A: Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch. Biochemistry 1996, 35:11036-11044
    • (1996) Biochemistry , vol.35 , pp. 11036-11044
    • Hanakam, F.1    Gerisch, G.2    Lotz, S.3    Alt, T.4    Seelig, A.5
  • 21
    • 0029113128 scopus 로고
    • The MARCKS family of protein kinase-C substrates
    • Aderem A: The MARCKS family of protein kinase-C substrates. Biochem. Soc. Transac. 1995, 23:587-591
    • (1995) Biochem. Soc. Transac. , vol.23 , pp. 587-591
    • Aderem, A.1
  • 22
    • 18744383090 scopus 로고    scopus 로고
    • Cytosolic acidification as a signal mediating hyperosmotic stress responses in Dictyostelium discoideum
    • Pintsch T, Satre M, Klein G, Schuster SC: Cytosolic acidification as a signal mediating hyperosmotic stress responses in Dictyostelium discoideum. BMC Cell Biol 2001, 2:9
    • (2001) BMC Cell Biol. , vol.2 , pp. 9
    • Pintsch, T.1    Satre, M.2    Klein, G.3    Schuster, S.C.4
  • 23
    • 0029828821 scopus 로고    scopus 로고
    • F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction
    • Liu G, Tang J, Edmonds BT, Murray J, Levin S, Condeelis J: F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction. J. Cell Biol. 1996, 135:953-963
    • (1996) J. Cell Biol. , vol.135 , pp. 953-963
    • Liu, G.1    Tang, J.2    Edmonds, B.T.3    Murray, J.4    Levin, S.5    Condeelis, J.6
  • 24
    • 0000672457 scopus 로고
    • Metabolic regulation via intracellular pH
    • Busa WB, Nuccitelli R: Metabolic regulation via intracellular pH. Am. J. Physiol. 1984, 246:R405-R438
    • (1984) Am. J. Physiol. , vol.246
    • Busa, W.B.1    Nuccitelli, R.2
  • 25
    • 0014843202 scopus 로고
    • Metabolism of the cellular slime mould Dictyostelium discoideum grown in axenic culture
    • Ashworth JM, Watts DJ: Metabolism of the cellular slime mould Dictyostelium discoideum grown in axenic culture. Biochem. J. 1970, 119:175-182
    • (1970) Biochem. J. , vol.119 , pp. 175-182
    • Ashworth, J.M.1    Watts, D.J.2
  • 26
    • 0029977873 scopus 로고    scopus 로고
    • Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: Intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein
    • Hanakam F, Albrecht R, Eckerskorn C, Matzner M, Gerisch G: Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein. EMBO J. 1996, 15:2935-2943
    • (1996) EMBO J. , vol.15 , pp. 2935-2943
    • Hanakam, F.1    Albrecht, R.2    Eckerskorn, C.3    Matzner, M.4    Gerisch, G.5
  • 27
    • 0029885430 scopus 로고    scopus 로고
    • Structure/function studies on the pH-dependent actin-binding protein hisactophilin in Dictyostelium mutants
    • Stoeckelhuber M, Noegel AA, Eckerskorn C, Kohler J, Rieger D, Schleicher M: Structure/function studies on the pH-dependent actin-binding protein hisactophilin in Dictyostelium mutants. J. Cell Sci. 1996, 109:1825-1835
    • (1996) J. Cell Sci. , vol.109 , pp. 1825-1835
    • Stoeckelhuber, M.1    Noegel, A.A.2    Eckerskorn, C.3    Kohler, J.4    Rieger, D.5    Schleicher, M.6
  • 28
    • 0001604571 scopus 로고
    • New actin-binding proteins from Dictyostelium discoideum
    • Schleicher M, Gerisch G, Isenberg G: New actin-binding proteins from Dictyostelium discoideum. EMBO J. 1984, 3:2095-2100
    • (1984) EMBO J. , vol.3 , pp. 2095-2100
    • Schleicher, M.1    Gerisch, G.2    Isenberg, G.3
  • 29
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos B, Marcandier S, Cozzone SJ: Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol 1991, 201:10-21
    • (1991) Methods Enzymol. , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, S.J.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochemistry 1976, 72:248-254
    • (1976) Anal. Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76:4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.