메뉴 건너뛰기




Volumn 288, Issue 32, 2013, Pages 23380-23393

Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN CYTOSKELETON; ATP-ASE ACTIVITY; ATPASES; CYTOSOLIC; DIRECT INTERACTIONS; FUNCTIONAL ASSAYS; POLYMERIZING ACTIN; SUBMEMBRANE;

EID: 84881469078     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.470542     Document Type: Article
Times cited : (22)

References (95)
  • 1
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler, E. E., and Zacharias, D. A. (2001) Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81, 21-50
    • (2001) Physiol. Rev. , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 2
    • 0023872238 scopus 로고
    • Identification and primary structure of a calmodulin binding domain of the Ca2pump of human erythrocytes
    • James, P., Maeda, M., Fischer, R., Verma, A. K., Krebs, J., Penniston, J. T., and Carafoli, E. (1988) Identification and primary structure of a calmodulin binding domain of the Ca2pump of human erythrocytes. J. Biol. Chem. 263, 2905-2910
    • (1988) J. Biol. Chem. , vol.263 , pp. 2905-2910
    • James, P.1    Maeda, M.2    Fischer, R.3    Verma, A.K.4    Krebs, J.5    Penniston, J.T.6    Carafoli, E.7
  • 3
    • 0024361269 scopus 로고
    • The calmodulin binding domain of the plasma membrane Ca2pump interacts both with calmodulin and with another part of the pump
    • Enyedi, A., Vorherr, T., James, P., McCormick, D. J., Filoteo, A. G., Carafoli, E., and Penniston, J. T. (1989) The calmodulin binding domain of the plasma membrane Ca2pump interacts both with calmodulin and with another part of the pump. J. Biol. Chem. 264, 12313-12321
    • (1989) J. Biol. Chem. , vol.264 , pp. 12313-12321
    • Enyedi, A.1    Vorherr, T.2    James, P.3    McCormick, D.J.4    Filoteo, A.G.5    Carafoli, E.6    Penniston, J.T.7
  • 4
    • 0019822476 scopus 로고
    • Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2-ATPase
    • Niggli, V., Adunyah, E. S., and Carafoli, E. (1981) Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2-ATPase. J. Biol. Chem. 256, 8588-8592
    • (1981) J. Biol. Chem. , vol.256 , pp. 8588-8592
    • Niggli, V.1    Adunyah, E.S.2    Carafoli, E.3
  • 6
    • 0022273846 scopus 로고
    • Phosphorylation of the Ca2-pumping ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase
    • Neyses, L., Reinlib, L., and Carafoli, E. (1985) Phosphorylation of the Ca2-pumping ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase. J. Biol. Chem. 260, 10283-10287
    • (1985) J. Biol. Chem. , vol.260 , pp. 10283-10287
    • Neyses, L.1    Reinlib, L.2    Carafoli, E.3
  • 7
    • 0032548035 scopus 로고    scopus 로고
    • Protein kinases A and C phosphorylate purified Ca2-ATPase from rat cortex, cerebellum, and hippocampus
    • Zylinska, L., Guerini, D., Gromadzinska, E., and Lachowicz, L. (1998) Protein kinases A and C phosphorylate purified Ca2-ATPase from rat cortex, cerebellum, and hippocampus. Biochim. Biophys. Acta 1448, 99-108
    • (1998) Biochim. Biophys. Acta , vol.1448 , pp. 99-108
    • Zylinska, L.1    Guerini, D.2    Gromadzinska, E.3    Lachowicz, L.4
  • 9
    • 0024165904 scopus 로고
    • Activation of the erythrocyte Ca2-ATPase by either self-association or interaction with calmodulin
    • Kosk-Kosicka, D., and Bzdega, T. (1988) Activation of the erythrocyte Ca2-ATPase by either self-association or interaction with calmodulin. J. Biol. Chem. 263, 18184-18189
    • (1988) J. Biol. Chem. , vol.263 , pp. 18184-18189
    • Kosk-Kosicka, D.1    Bzdega, T.2
  • 10
    • 0019308996 scopus 로고
    • Characteristics and regulation of active calcium transport in inside-out red cell membrane vesicles
    • Sarkadi, B., Szász, I., and Gárdos, G. (1980) Characteristics and regulation of active calcium transport in inside-out red cell membrane vesicles. Biochim. Biophys. Acta 598, 326-338
    • (1980) Biochim. Biophys. Acta , vol.598 , pp. 326-338
    • Sarkadi, B.1    Szász, I.2    Gárdos, G.3
  • 11
    • 34249088614 scopus 로고    scopus 로고
    • Plasma membrane calcium pump activity is affected by the membrane protein concentration: Evidence for the involvement of the actin cytoskeleton
    • Vanagas, L., Rossi, R. C., Caride, A. J., Filoteo, A. G., Strehler, E. E., and Rossi, J. P. (2007) Plasma membrane calcium pump activity is affected by the membrane protein concentration: evidence for the involvement of the actin cytoskeleton. Biochim. Biophys. Acta 1768, 1641-1649
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1641-1649
    • Vanagas, L.1    Rossi, R.C.2    Caride, A.J.3    Filoteo, A.G.4    Strehler, E.E.5    Rossi, J.P.6
  • 13
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison, T. J., and Cramer, L. P. (1996) Actin-based cell motility and cell locomotion. Cell 84, 371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 15
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann, B., Kessels, M. M., and Kelly, R. B. (2000) Molecular links between endocytosis and the actin cytoskeleton. J. Cell Biol. 150, F111-F116
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 16
    • 0034306013 scopus 로고    scopus 로고
    • Function of Rho family proteins in actin dynamics during phagocytosis and engulfment
    • Chimini, G., and Chavrier, P. (2000) Function of Rho family proteins in actin dynamics during phagocytosis and engulfment. Nat. Cell Biol. 2, E191-E196
    • (2000) Nat. Cell Biol. , vol.2
    • Chimini, G.1    Chavrier, P.2
  • 17
    • 0033974762 scopus 로고    scopus 로고
    • Microtubuleactomyosin interactions in cortical flow and cytokinesis
    • Mandato, C. A., Benink, H. A., and Bement, W. M. (2000) Microtubuleactomyosin interactions in cortical flow and cytokinesis. Cell Motil. Cytoskeleton 45, 87-92
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 87-92
    • Mandato, C.A.1    Benink, H.A.2    Bement, W.M.3
  • 18
    • 0033961421 scopus 로고    scopus 로고
    • Actin coating of secretory granules during regulated exocytosis correlates with the release of rab3D
    • Valentijn, J. A., Valentijn, K., Pastore, L. M., and Jamieson, J. D. (2000) Actin coating of secretory granules during regulated exocytosis correlates with the release of rab3D. Proc. Natl. Acad. Sci. U.S.A. 97, 1091-1095
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1091-1095
    • Valentijn, J.A.1    Valentijn, K.2    Pastore, L.M.3    Jamieson, J.D.4
  • 19
    • 0034669644 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in regulation of ion transport: Examples from epithelial cells
    • Khurana, S. (2000) Role of actin cytoskeleton in regulation of ion transport: examples from epithelial cells. J. Membr. Biol. 178, 73-87
    • (2000) J. Membr. Biol. , vol.178 , pp. 73-87
    • Khurana, S.1
  • 23
    • 0028822397 scopus 로고
    • Actin filaments stimulate the Na-K-ATPase
    • Cantiello, H. F. (1995) Actin filaments stimulate the Na-K-ATPase. Am. J. Physiol. 269, F637-F643
    • (1995) Am. J. Physiol. , vol.269
    • Cantiello, H.F.1
  • 26
    • 0027489905 scopus 로고
    • Focusing on unpolymerized actin
    • Fechheimer, M., and Zigmond, S. (1993) Focusing on unpolymerized actin. J. Cell Biol. 123, 1-5
    • (1993) J. Cell Biol. , vol.123 , pp. 1-5
    • Fechheimer, M.1    Zigmond, S.2
  • 27
    • 0023839692 scopus 로고
    • Unfertilized sea urchin eggs contain a discrete cortical shell of actin that is subdivided into two organizational states
    • Spudich, A., Wrenn, J. T., and Wessells, N. K. (1988) Unfertilized sea urchin eggs contain a discrete cortical shell of actin that is subdivided into two organizational states. Cell Motil. Cytoskeleton 9, 85-96
    • (1988) Cell Motil. Cytoskeleton , vol.9 , pp. 85-96
    • Spudich, A.1    Wrenn, J.T.2    Wessells, N.K.3
  • 28
    • 0024353743 scopus 로고
    • The cortical actin-membrane cytoskeleton of unfertilized sea urchin eggs: Analysis of the spatial organization and relationship of filamentous actin, nonfilamentous actin, and egg spectrin
    • Bonder, E. M., Fishkind, D. J., Cotran, N. M., and Begg, D. A. (1989) The cortical actin-membrane cytoskeleton of unfertilized sea urchin eggs: analysis of the spatial organization and relationship of filamentous actin, nonfilamentous actin, and egg spectrin. Dev. Biol. 134, 327-341
    • (1989) Dev. Biol. , vol.134 , pp. 327-341
    • Bonder, E.M.1    Fishkind, D.J.2    Cotran, N.M.3    Begg, D.A.4
  • 29
    • 34249052338 scopus 로고    scopus 로고
    • "actin" g on GLUT4: Membrane & cytoskeletal components of insulin secretion
    • Brozinick, J. T., Jr., Berkemeier, B. A., and Elmendorf, J. S. (2007) "Actin" g on GLUT4: membrane & cytoskeletal components of insulin secretion. Curr. Diabetes Rev. 3, 111-122
    • (2007) Curr. Diabetes Rev. , vol.3 , pp. 111-122
    • Brozinick Jr., J.T.1    Berkemeier, B.A.2    Elmendorf, J.S.3
  • 30
    • 39149109271 scopus 로고    scopus 로고
    • IRSp53: Crossing the road of membrane and actin dynamics in the formation of membrane protusions
    • Scita, G., Confalonieri, S., Lappalainen, P., and Suetsugu, S. (2008) IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protusions. Trends Cell Biol. 18, 52-60
    • (2008) Trends Cell Biol. , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4
  • 31
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: Coupling membrane dynamics to cortical actin assembly
    • Weed, S. A., and Parsons, J. T. (2001) Cortactin:coupling membrane dynamics to cortical actin assembly. Oncogene 20, 6418-6434
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 32
    • 34047117842 scopus 로고    scopus 로고
    • T-cell receptor-dependent actin regulatory mechanisms
    • Huang, Y., and Burkhardt, J. K. (2007) T-cell receptor-dependent actin regulatory mechanisms. J. Cell Sci. 120, 723-730
    • (2007) J. Cell Sci. , vol.120 , pp. 723-730
    • Huang, Y.1    Burkhardt, J.K.2
  • 33
    • 33749533257 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics at the immune synapse: New stars join the actin troupe
    • Billadeau, D. D., and Burkhardt, J. K. (2006) Regulation of cytoskeletal dynamics at the immune synapse: new stars join the actin troupe. Traffic 11, 1451-1460
    • (2006) Traffic , vol.11 , pp. 1451-1460
    • Billadeau, D.D.1    Burkhardt, J.K.2
  • 35
    • 0141961569 scopus 로고    scopus 로고
    • Expression, purification, and characterization of isoform 1 of the plasma membrane Ca2pump: Focus on calpain sensitivity
    • Guerini, D., Pan, B., and Carafoli, E. (2003) Expression, purification, and characterization of isoform 1 of the plasma membrane Ca2pump: focus on calpain sensitivity. J. Biol. Chem. 278, 38141-38148
    • (2003) J. Biol. Chem. , vol.278 , pp. 38141-38148
    • Guerini, D.1    Pan, B.2    Carafoli, E.3
  • 36
    • 0018654140 scopus 로고
    • Purification of the (Ca2-Mg2)-ATPase from human erythrocyte membranes using a calmodulin affinity column
    • Niggli, V., Penniston, J. T., and Carafoli, E. (1979) Purification of the (Ca2-Mg2)-ATPase from human erythrocyte membranes using a calmodulin affinity column. J. Biol. Chem. 254, 9955-9958
    • (1979) J. Biol. Chem. , vol.254 , pp. 9955-9958
    • Niggli, V.1    Penniston, J.T.2    Carafoli, E.3
  • 37
    • 0037591275 scopus 로고    scopus 로고
    • Onthe mechanism of activation of the plasma membrane Ca2-ATPase by ATP and acidic phospholipids
    • Filomatori, C. V., and Rega, A. F. (2003)Onthe mechanism of activation of the plasma membrane Ca2-ATPase by ATP and acidic phospholipids. J. Biol. Chem. 278, 22265-22271
    • (2003) J. Biol. Chem. , vol.278 , pp. 22265-22271
    • Filomatori, C.V.1    Rega, A.F.2
  • 40
    • 0031968344 scopus 로고    scopus 로고
    • Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers
    • Xu, J., Schwarz, W. H., Käs, J. A., Stossel, T. P., Janmey, P. A., and Pollard, T. D. (1998) Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers. Biophys. J. 74, 2731-2740
    • (1998) Biophys. J. , vol.74 , pp. 2731-2740
    • Xu, J.1    Schwarz, W.H.2    Käs, J.A.3    Stossel, T.P.4    Janmey, P.A.5    Pollard, T.D.6
  • 41
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., LöfAs, S., and Lindquist, G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268-277
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfas, S.2    Lindquist, G.3
  • 44
    • 0020533805 scopus 로고
    • Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization
    • Cooper, J. A., Walker, S. B., and Pollard, T. D. (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4, 253-262
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 45
    • 0018144260 scopus 로고
    • Two classes of site for ATP in the Ca2-ATPase from human red cell membranes
    • Richards, D. E., Rega, A. F., and Garrahan, P. J. (1978) Two classes of site for ATP in the Ca2-ATPase from human red cell membranes. Biochim. Biophys. Acta 511, 194-201
    • (1978) Biochim. Biophys. Acta , vol.511 , pp. 194-201
    • Richards, D.E.1    Rega, A.F.2    Garrahan, P.J.3
  • 46
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M. R. (1992) A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. U.S.A. 89, 4884-4887
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 47
    • 0035865263 scopus 로고    scopus 로고
    • Quantitation of plasma membrane calcium pump phosphorylated intermediates by electrophoresis
    • Echarte, M. M., Levi, V., Villamil, A. M., Rossi, R. C., and Rossi, J. P. (2001) Quantitation of plasma membrane calcium pump phosphorylated intermediates by electrophoresis. Anal. Biochem. 289, 267-273
    • (2001) Anal. Biochem. , vol.289 , pp. 267-273
    • Echarte, M.M.1    Levi, V.2    Villamil, A.M.3    Rossi, R.C.4    Rossi, J.P.5
  • 48
    • 0020631637 scopus 로고
    • The effects of alkali metal ions on active Ca2transport in reconstituted ghosts from human red cells
    • Kratje, R. B., Garrahan, P. J., and Rega, A. F. (1983) The effects of alkali metal ions on active Ca2transport in reconstituted ghosts from human red cells. Biochim. Biophys. Acta 731, 40-46
    • (1983) Biochim. Biophys. Acta , vol.731 , pp. 40-46
    • Kratje, R.B.1    Garrahan, P.J.2    Rega, A.F.3
  • 49
    • 64149118900 scopus 로고    scopus 로고
    • A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2pumps revealed by a photoactivatable phospholipidic probe
    • Mangialavori, I., Giraldo, A. M., Buslje, C. M., Gomes, M. F., Caride, A. J., and Rossi, J. P. (2009) A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2pumps revealed by a photoactivatable phospholipidic probe. J. Biol. Chem. 284, 4823-4828
    • (2009) J. Biol. Chem. , vol.284 , pp. 4823-4828
    • Mangialavori, I.1    Giraldo, A.M.2    Buslje, C.M.3    Gomes, M.F.4    Caride, A.J.5    Rossi, J.P.6
  • 50
    • 0024316826 scopus 로고
    • Fluorescence energy transfer studies of purified erythrocyte Ca2-ATPase. Ca2-regulated activation by oligomerization
    • Kosk-Kosicka, D., Bzdega, T., and Wawrzynow, A. (1989) Fluorescence energy transfer studies of purified erythrocyte Ca2-ATPase. Ca2-regulated activation by oligomerization. J. Biol. Chem. 264, 19495-19499
    • (1989) J. Biol. Chem. , vol.264 , pp. 19495-19499
    • Kosk-Kosicka, D.1    Bzdega, T.2    Wawrzynow, A.3
  • 51
    • 0029914614 scopus 로고    scopus 로고
    • The active species of plasma membrane Ca2-ATPase are a dimer and a monomer-calmodulin complex
    • Sackett, D. L., and Kosk-Kosicka, D. (1996) The active species of plasma membrane Ca2-ATPase are a dimer and a monomer-calmodulin complex. J. Biol. Chem. 271, 9987-9991
    • (1996) J. Biol. Chem. , vol.271 , pp. 9987-9991
    • Sackett, D.L.1    Kosk-Kosicka, D.2
  • 53
    • 33745902222 scopus 로고    scopus 로고
    • Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology
    • Navratilova, I., Dioszegi, M., and Myszka, D. G. (2006) Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology. Anal. Biochem. 355, 132-139
    • (2006) Anal. Biochem. , vol.355 , pp. 132-139
    • Navratilova, I.1    Dioszegi, M.2    Myszka, D.G.3
  • 54
    • 0032530540 scopus 로고    scopus 로고
    • Modulation of the plasma membrane Ca2pump
    • Penniston, J. T., and Enyedi, A. (1998) Modulation of the plasma membrane Ca2pump. J. Membr. Biol. 165, 101-109
    • (1998) J. Membr. Biol. , vol.165 , pp. 101-109
    • Penniston, J.T.1    Enyedi, A.2
  • 55
    • 1942421320 scopus 로고    scopus 로고
    • Calcium pumps of plasma membrane and cell interior
    • Strehler, E. E., and Treiman, M. (2004) Calcium pumps of plasma membrane and cell interior. Curr. Mol. Med. 4, 323-335
    • (2004) Curr. Mol. Med. , vol.4 , pp. 323-335
    • Strehler, E.E.1    Treiman, M.2
  • 56
    • 0035953757 scopus 로고    scopus 로고
    • Structure of the gating domain of a Ca2-activated Kchannel complexed with Ca2/calmodulin
    • Schumacher, M. A., Rivard, A. F., Bächinger, H. P., and Adelman, J. P. (2001) Structure of the gating domain of a Ca2-activated Kchannel complexed with Ca2/calmodulin. Nature 410, 1120-1124
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.A.1    Rivard, A.F.2    Bächinger, H.P.3    Adelman, J.P.4
  • 57
    • 0022978478 scopus 로고
    • Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis
    • Sarkadi, B., Enyedi, A., Földes-Papp, Z., and Gárdos, G. (1986) Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis. J. Biol. Chem. 261, 9552-9557
    • (1986) J. Biol. Chem. , vol.261 , pp. 9552-9557
    • Sarkadi, B.1    Enyedi, A.2    Földes-Papp, Z.3    Gárdos, G.4
  • 58
    • 0026710613 scopus 로고
    • The lipid-binding peptide from the plasma membrane Ca2pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid
    • Filoteo, A. G., Enyedi, A., and Penniston, J. T. (1992) The lipid-binding peptide from the plasma membrane Ca2pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid. J. Biol. Chem. 267, 11800-11805
    • (1992) J. Biol. Chem. , vol.267 , pp. 11800-11805
    • Filoteo, A.G.1    Enyedi, A.2    Penniston, J.T.3
  • 59
    • 0025357327 scopus 로고
    • Effects of calmodulin on erythrocyte Ca2-ATPase activation and oligomerization
    • Kosk-Kosicka, D., and Bzdega, T. (1990) Effects of calmodulin on erythrocyte Ca2-ATPase activation and oligomerization. Biochemistry 29, 3772-3777
    • (1990) Biochemistry , vol.29 , pp. 3772-3777
    • Kosk-Kosicka, D.1    Bzdega, T.2
  • 60
    • 0025089832 scopus 로고
    • Fluorescence studies on calmodulin binding to erythrocyte Ca2-ATPase in different oligomerization states
    • Kosk-Kosicka, D., Bzdega, T., and Johnson, J. D. (1990) Fluorescence studies on calmodulin binding to erythrocyte Ca2-ATPase in different oligomerization states. Biochemistry 29, 1875-1879
    • (1990) Biochemistry , vol.29 , pp. 1875-1879
    • Kosk-Kosicka, D.1    Bzdega, T.2    Johnson, J.D.3
  • 61
    • 0026074356 scopus 로고
    • The calmodulin-binding domain mediates the self-association of the plasma membrane Ca2pump
    • Vorherr, T., Kessler, T., Hofmann, F., and Carafoli, E. (1991) The calmodulin-binding domain mediates the self-association of the plasma membrane Ca2pump. J. Biol. Chem. 266, 22-27
    • (1991) J. Biol. Chem. , vol.266 , pp. 22-27
    • Vorherr, T.1    Kessler, T.2    Hofmann, F.3    Carafoli, E.4
  • 63
    • 0021259215 scopus 로고
    • The rate constant for ATP hydrolysis by polymerized actin
    • Pollard, T. D., and Weeds, A. G. (1984) The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett. 170, 94-98
    • (1984) FEBS Lett. , vol.170 , pp. 94-98
    • Pollard, T.D.1    Weeds, A.G.2
  • 64
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn, E. D., Carlier, M. F., and Pantaloni, D. (1987) Actin polymerization and ATP hydrolysis. Science 238, 638-644
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.F.2    Pantaloni, D.3
  • 65
    • 0025753377 scopus 로고
    • Nucleotide hydrolysis in cytoskeletal assembly
    • Carlier, M. F. (1991) Nucleotide hydrolysis in cytoskeletal assembly. Curr. Opin. Cell Biol. 3, 12-17
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 12-17
    • Carlier, M.F.1
  • 66
    • 0022930094 scopus 로고
    • Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin
    • Carlier, M. F., Pantaloni, D., and Korn, E. D. (1986) Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin. J. Biol. Chem. 261, 10785-10792
    • (1986) J. Biol. Chem. , vol.261 , pp. 10785-10792
    • Carlier, M.F.1    Pantaloni, D.2    Korn, E.D.3
  • 68
    • 0016785533 scopus 로고
    • Ca2-stimulated membrane phosphorylation and ATPase activity of the human erythrocyte
    • Katz, S., and Blostein, R. (1975) Ca2-stimulated membrane phosphorylation and ATPase activity of the human erythrocyte. Biochim. Biophys. Acta 389, 314-324
    • (1975) Biochim. Biophys. Acta , vol.389 , pp. 314-324
    • Katz, S.1    Blostein, R.2
  • 69
    • 0019318034 scopus 로고
    • Characterization of the phosphorylated intermediate of the isolated high-affinity (Ca2-Mg2)-ATPase of human erythrocyte membranes
    • Lichtner, R., and Wolf, H. U. (1980) Characterization of the phosphorylated intermediate of the isolated high-affinity (Ca2-Mg2)-ATPase of human erythrocyte membranes. Biochim. Biophys. Acta 598, 486-493
    • (1980) Biochim. Biophys. Acta , vol.598 , pp. 486-493
    • Lichtner, R.1    Wolf, H.U.2
  • 71
    • 0037081821 scopus 로고    scopus 로고
    • Pre-steady-state phosphorylation and dephosphorylation of detergent-purified plasma-membrane Ca2-ATPase
    • Bredeston, L. M., and Rega, A. F. (2002) Pre-steady-state phosphorylation and dephosphorylation of detergent-purified plasma-membrane Ca2-ATPase. Biochem. J. 361, 355-361
    • (2002) Biochem. J. , vol.361 , pp. 355-361
    • Bredeston, L.M.1    Rega, A.F.2
  • 72
    • 73649146199 scopus 로고    scopus 로고
    • Determination of the dissociation constants for Ca2and calmodulin from the plasma membrane Ca2pump by a lipid probe that senses membrane domain changes
    • Mangialavori, I., Ferreira-Gomes, M., Pignataro, M. F., Strehler, E. E., and Rossi, J. P. (2010) Determination of the dissociation constants for Ca2and calmodulin from the plasma membrane Ca2pump by a lipid probe that senses membrane domain changes. J. Biol. Chem. 285, 123-130
    • (2010) J. Biol. Chem. , vol.285 , pp. 123-130
    • Mangialavori, I.1    Ferreira-Gomes, M.2    Pignataro, M.F.3    Strehler, E.E.4    Rossi, J.P.5
  • 73
    • 79956294725 scopus 로고    scopus 로고
    • Plasma membrane calcium pump (PMCA) differential exposure of hydrophobic domains after calmodulin and phosphatidic acid activation
    • Mangialavori, I., Villamil-Giraldo, A. M., Pignataro, M. F., Ferreira-Gomes, M., Caride, A. J., and Rossi, J. P. (2011) Plasma membrane calcium pump (PMCA) differential exposure of hydrophobic domains after calmodulin and phosphatidic acid activation. J. Biol. Chem. 286, 18397-18404
    • (2011) J. Biol. Chem. , vol.286 , pp. 18397-18404
    • Mangialavori, I.1    Villamil-Giraldo, A.M.2    Pignataro, M.F.3    Ferreira-Gomes, M.4    Caride, A.J.5    Rossi, J.P.6
  • 74
    • 79953792525 scopus 로고    scopus 로고
    • Diving into the lipid bilayer to investigate the transmembrane organization and conformational state transitions of P-type ion ATPases
    • Mangialavori, I. C., Caride, A. J., Rossi, R. C., Rossi, J. P., and Strehler, E. E. (2011) Diving into the lipid bilayer to investigate the transmembrane organization and conformational state transitions of P-type ion ATPases. Curr. Chem. Biol. 5, 118-129
    • (2011) Curr. Chem. Biol. , vol.5 , pp. 118-129
    • Mangialavori, I.C.1    Caride, A.J.2    Rossi, R.C.3    Rossi, J.P.4    Strehler, E.E.5
  • 75
    • 0021932820 scopus 로고
    • Cooperative calcium binding and calmodulin regulation in the calcium-dependent adenosine triphosphatase purified from the erythrocyte membrane
    • Kosk-Kosicka, D., and Inesi, G. (1985) Cooperative calcium binding and calmodulin regulation in the calcium-dependent adenosine triphosphatase purified from the erythrocyte membrane. FEBS Lett. 189, 67-71
    • (1985) FEBS Lett. , vol.189 , pp. 67-71
    • Kosk-Kosicka, D.1    Inesi, G.2
  • 76
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. (1993) Calcium pump of the plasma membrane is localized in caveolae. J. Cell Biol. 120, 1147-1157
    • (1993) J. Cell Biol. , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 77
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • Pike, L. J., and Casey, L. (1996) Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem. 271, 26453-26456
    • (1996) J. Biol. Chem. , vol.271 , pp. 26453-26456
    • Pike, L.J.1    Casey, L.2
  • 79
    • 33748747144 scopus 로고    scopus 로고
    • Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components
    • Head, B. P., Patel, H. H., Roth, D. M., Murray, F., Swaney, J. S., Niesman, I. R., Farquhar, M. G., and Insel, P. A. (2006) Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components. J. Biol. Chem. 281, 26391-26399
    • (2006) J. Biol. Chem. , vol.281 , pp. 26391-26399
    • Head, B.P.1    Patel, H.H.2    Roth, D.M.3    Murray, F.4    Swaney, J.S.5    Niesman, I.R.6    Farquhar, M.G.7    Insel, P.A.8
  • 80
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • Carafoli, E. (1987) Intracellular calcium homeostasis. Annu. Rev. Biochem. 56, 395-433
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 81
    • 33646772190 scopus 로고    scopus 로고
    • Direct measurement of VDAC-actin interaction by surface plasmon resonance
    • Roman, I., Figys, J., Steurs, G., and Zizi, M. (2006) Direct measurement of VDAC-actin interaction by surface plasmon resonance. Biochim. Biophys. Acta 1758, 479-486
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 479-486
    • Roman, I.1    Figys, J.2    Steurs, G.3    Zizi, M.4
  • 83
    • 0016698509 scopus 로고
    • Kinetics of the cooperative association of actin to actin filaments
    • Wegner, A., and Engel, J. (1975) Kinetics of the cooperative association of actin to actin filaments. Biophys. Chem. 3, 215-225
    • (1975) Biophys. Chem. , vol.3 , pp. 215-225
    • Wegner, A.1    Engel, J.2
  • 84
    • 0021099326 scopus 로고
    • The kinetics of actin nucleation and polymerization
    • Tobacman, L. S., and Korn, E. D. (1983) The kinetics of actin nucleation and polymerization. J. Biol. Chem. 258, 3207-3214
    • (1983) J. Biol. Chem. , vol.258 , pp. 3207-3214
    • Tobacman, L.S.1    Korn, E.D.2
  • 85
    • 0024457508 scopus 로고
    • From signal to pseudopod. How cells control cytoplasmic actin assembly
    • Stossel, T. P. (1989) From signal to pseudopod. How cells control cytoplasmic actin assembly. J. Biol. Chem. 264, 18261-18264
    • (1989) J. Biol. Chem. , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 86
    • 0019729339 scopus 로고
    • Ca2control of actin filament length. Effects of macrophage gelsolin on actin polymerization
    • Yin, H. L., Hartwig, J. H., Maruyama, K., and Stossel, T. P. (1981) Ca2control of actin filament length. Effects of macrophage gelsolin on actin polymerization. J. Biol. Chem. 256, 9693-9697
    • (1981) J. Biol. Chem. , vol.256 , pp. 9693-9697
    • Yin, H.L.1    Hartwig, J.H.2    Maruyama, K.3    Stossel, T.P.4
  • 87
    • 0018869290 scopus 로고
    • Villin is a major protein of the microvillus cytoskeleton which binds bothGand F actin in a calcium-dependent manner
    • Bretscher, A., and Weber, K. (1980) Villin is a major protein of the microvillus cytoskeleton which binds bothGand F actin in a calcium-dependent manner. Cell 20, 839-847
    • (1980) Cell , vol.20 , pp. 839-847
    • Bretscher, A.1    Weber, K.2
  • 88
    • 48249121534 scopus 로고    scopus 로고
    • Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers
    • Kueh, H. Y., Charras, G. T., Mitchison, T. J., and Brieher, W. M. (2008) Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. J. Cell Biol. 182, 341-353
    • (2008) J. Cell Biol. , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Mitchison, T.J.3    Brieher, W.M.4
  • 90
    • 0026101038 scopus 로고
    • Identification of the site important for the actinactivated MgATPase activity of myosin subfragment-1
    • Yamamoto, K. (1991) Identification of the site important for the actinactivated MgATPase activity of myosin subfragment-1. J. Mol. Biol. 217, 229-233
    • (1991) J. Mol. Biol. , vol.217 , pp. 229-233
    • Yamamoto, K.1
  • 91
    • 0025856003 scopus 로고
    • Thymosin 4 and Fx, an actin-sequestering peptide, are indistinguishable
    • Safer, D., Elzinga, M., and Nachmias, V. T. (1991) Thymosin 4 and Fx, an actin-sequestering peptide, are indistinguishable. J. Biol. Chem. 266, 4029-4032
    • (1991) J. Biol. Chem. , vol.266 , pp. 4029-4032
    • Safer, D.1    Elzinga, M.2    Nachmias, V.T.3
  • 92
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J., and Louvard, D. (1992) An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell 70, 81-92
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 93
    • 0033010590 scopus 로고    scopus 로고
    • Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin
    • Kusano, K., Abe, H., and Obinata, T. (1999) Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin. Mol. Cell. Biochem. 190, 133-141
    • (1999) Mol. Cell. Biochem. , vol.190 , pp. 133-141
    • Kusano, K.1    Abe, H.2    Obinata, T.3
  • 94
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C
    • Goldschmidt-Clermont, P. J., Machesky, L. M., Baldassare, J. J., and Pollard, T. D. (1990) The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575-1578
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    Machesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 95
    • 0028823009 scopus 로고
    • Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: Behavior in solutions of mixed solvent and anionic micelles
    • Xian, W., Vegners, R., Janmey, P. A., and Braunlin, W. H. (1995) Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles. Biophys. J. 69, 2695-2702
    • (1995) Biophys. J. , vol.69 , pp. 2695-2702
    • Xian, W.1    Vegners, R.2    Janmey, P.A.3    Braunlin, W.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.