메뉴 건너뛰기




Volumn 25, Issue 1, 2000, Pages 133-144

Scinderin, a Ca2+-dependent actin filament severing protein that controls cortical actin network dynamics during secretion

Author keywords

Actin; Ca2+; Chromaffin cell; Exocytosis; PIP2; Platelet; Scinderin

Indexed keywords

CALCIUM ION; F ACTIN; RECOMBINANT PROTEIN; ACTIN; ACTIN BINDING PROTEIN; CALCIUM; GELSOLIN; SCINDERIN;

EID: 0033621875     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1007503919265     Document Type: Article
Times cited : (30)

References (53)
  • 2
    • 0000466199 scopus 로고
    • Common properties in the mechanisms of synthesis, processing and storage of secretory products
    • Poisner, A. M., and Trifaró, J-M. (eds.) The Secretory Granule. Elsevier/ North Holland
    • Trifaró, J-M., and Poisner, A. M. 1982. Common properties in the mechanisms of synthesis, processing and storage of secretory products. Pages 387-407, in Poisner, A. M., and Trifaró, J-M. (eds.) The Secretory Process. The Secretory Granule. Elsevier/ North Holland.
    • (1982) The Secretory Process , pp. 387-407
    • Trifaró, J.-M.1    Poisner, A.M.2
  • 4
    • 0027409301 scopus 로고
    • Multiple calcium-dependent processes related to secretion in bovine chromaffin cells
    • Neher, E., and Zucker, R. S. 1993. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron 10:21-30.
    • (1993) Neuron , vol.10 , pp. 21-30
    • Neher, E.1    Zucker, R.S.2
  • 5
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale, M. L., Seward, E. P., and Trifaró, J-M. 1995. Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron, 14:353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaró, J.-M.3
  • 6
    • 0025840196 scopus 로고
    • Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin
    • Vitale, M. L., Rodríguez Del Castillo, A., Tchakarov, L., and Trifaró, J-M. 1991. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J. Cell Biol. 113:1057-1067.
    • (1991) J. Cell Biol. , vol.113 , pp. 1057-1067
    • Vitale, M.L.1    Rodríguez Del Castillo, A.2    Tchakarov, L.3    Trifaró, J.-M.4
  • 7
    • 0020328662 scopus 로고
    • Dissection of stages in exocytosis in the adrenal chromaffin cells with use of trifluoperazine
    • Burgoyne, R. D., Geisow, M. J., and Barron, J. 1982. Dissection of stages in exocytosis in the adrenal chromaffin cells with use of trifluoperazine. Proc. R. Soc. Lond.(B)216:111-115.
    • (1982) Proc. R. Soc. Lond.(B) , vol.216 , pp. 111-115
    • Burgoyne, R.D.1    Geisow, M.J.2    Barron, J.3
  • 8
    • 0028862292 scopus 로고
    • Docked granules, the exocytotic burst, and the need for ATP hydrolysis in endocrine cells
    • Parsons, T. D., Coorssen, J. R., Horstmann, H., and Almers, W. 1995. Docked granules, the exocytotic burst, and the need for ATP hydrolysis in endocrine cells. Neuron 15:1085-1096.
    • (1995) Neuron , vol.15 , pp. 1085-1096
    • Parsons, T.D.1    Coorssen, J.R.2    Horstmann, H.3    Almers, W.4
  • 9
    • 0026709643 scopus 로고
    • Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components
    • Bittner, M. A., and Holz, R. W. 1992. Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J. Biol. Chem. 267:16219-16225.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16219-16225
    • Bittner, M.A.1    Holz, R.W.2
  • 10
    • 0025828234 scopus 로고
    • Proteins of synaptic vesicles involved in exocytosis and membrane recycling
    • Sudhof, T. C., and Jahn, R. 1991. Proteins of synaptic vesicles involved in exocytosis and membrane recycling. Neuron 6:665-677.
    • (1991) Neuron , vol.6 , pp. 665-677
    • Sudhof, T.C.1    Jahn, R.2
  • 11
    • 0027269605 scopus 로고
    • Inhibition of neurotransmitter release by C 2-domain peptides implicates synaptotagmin in exocytosis
    • Bommert, K., Charlton, M. P., DeBello, W. M., Chin, G. J., Betz, H., and Augustine, G. J. 1993. Inhibition of neurotransmitter release by C 2-domain peptides implicates synaptotagmin in exocytosis. Nature 363:163-165.
    • (1993) Nature , vol.363 , pp. 163-165
    • Bommert, K.1    Charlton, M.P.2    DeBello, W.M.3    Chin, G.J.4    Betz, H.5    Augustine, G.J.6
  • 12
    • 0027197065 scopus 로고
    • Synaptotagmin: A calcium-sensitive inhibitior of exocytosis?
    • Popov, S. V., and Poo, M. M. 1993. Synaptotagmin: a calcium-sensitive inhibitior of exocytosis? Cell 73:1247-1249.
    • (1993) Cell , vol.73 , pp. 1247-1249
    • Popov, S.V.1    Poo, M.M.2
  • 13
    • 0027238820 scopus 로고
    • Release of secretory products during transient vesicle fusion
    • Alvarez de Toledo, G., Fernández-Chacón, R., and Fernández, J. M. 1993. Release of secretory products during transient vesicle fusion. Nature 363:554-557.
    • (1993) Nature , vol.363 , pp. 554-557
    • Alvarez De Toledo, G.1    Fernández-Chacón, R.2    Fernández, J.M.3
  • 14
    • 0027489573 scopus 로고
    • Cytoskeleton dynamics during neurotransmitter release
    • Trifaró, J-M., and Vitale, M. L. 1993. Cytoskeleton dynamics during neurotransmitter release. Trends Neurosci. 16:466-472.
    • (1993) Trends Neurosci. , vol.16 , pp. 466-472
    • Trifaró, J.-M.1    Vitale, M.L.2
  • 15
    • 0000231271 scopus 로고
    • The cultured chromaffin cell: A model for the study of biology and pharmacology of paraneurons
    • Trifaró, J-M. 1982. The cultured chromaffin cell: a model for the study of biology and pharmacology of paraneurons. Trends in Pharmacol. Sci. 3:389-392.
    • (1982) Trends in Pharmacol. Sci. , vol.3 , pp. 389-392
    • Trifaró, J.-M.1
  • 16
    • 0000722168 scopus 로고
    • The adrenal paraneuron, its biology and pharmacology
    • Trifaró, J-M. 1984. The adrenal paraneuron, its biology and pharmacology. Can. J. Physiol. Pharmacol. 62:465-466.
    • (1984) Can. J. Physiol. Pharmacol. , vol.62 , pp. 465-466
    • Trifaró, J.-M.1
  • 17
    • 0014353877 scopus 로고
    • Stimulus-secretion coupling: The concept and clues from chromaffin and other cells
    • Douglas, W. W. 1968. Stimulus-secretion coupling: The concept and clues from chromaffin and other cells. Br. J. Pharmacol. 34:451-474.
    • (1968) Br. J. Pharmacol. , vol.34 , pp. 451-474
    • Douglas, W.W.1
  • 18
    • 73049146627 scopus 로고
    • The role of calcium in the secretory response of the adrenal medulla to acetylcholine
    • Douglas, W. W., and Rubin, R. P. 1961. The role of calcium in the secretory response of the adrenal medulla to acetylcholine. J. Physiol. 159:40-57.
    • (1961) J. Physiol. , vol.159 , pp. 40-57
    • Douglas, W.W.1    Rubin, R.P.2
  • 19
    • 84944496766 scopus 로고
    • Calcium and synaptic transmission in a sympathetic ganglion
    • Harvey, D. G., and Maclntoch, F. C. 1940. Calcium and synaptic transmission in a sympathetic ganglion. J. Physiol. 97:408-418.
    • (1940) J. Physiol. , vol.97 , pp. 408-418
    • Harvey, D.G.1    Maclntoch, F.C.2
  • 20
    • 0009532956 scopus 로고
    • Excitabilité des fibres adrénaline-sécrétories du neuf grand splanchnique: Fréquences, seuil et optimum des stimulus: rôle de l'ion calcium
    • Houssay, B. A., and Molinelli, E. A. 1928. Excitabilité des fibres adrénaline-sécrétories du neuf grand splanchnique: fréquences, seuil et optimum des stimulus: rôle de l'ion calcium. C. R. Seances Soc. Biol. Ses Fil. 99:172-174.
    • (1928) C. R. Seances Soc. Biol. Ses Fil. , vol.99 , pp. 172-174
    • Houssay, B.A.1    Molinelli, E.A.2
  • 23
    • 0022568973 scopus 로고
    • Secretory cell actin-binding proteins identification of gelsolin-like protein in chromaffin cells
    • Bader, M-F., Trifaró, J-M., Langley, O. K., Thiersé, D., and Aunis, D. 1986. Secretory cell actin-binding proteins identification of gelsolin-like protein in chromaffin cells. J. Cell Biol. 102:636-646.
    • (1986) J. Cell Biol. , vol.102 , pp. 636-646
    • Bader, M.-F.1    Trifaró, J.-M.2    Langley, O.K.3    Thiersé, D.4    Aunis, D.5
  • 25
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium dependent regulatory protein
    • Yin, H., and Stossel, T. P. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium dependent regulatory protein. Nature 281:583-586.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.1    Stossel, T.P.2
  • 26
    • 0019751470 scopus 로고
    • Identification of gelsolin, a calcium-dependent regulatory protein of actin gel-sol transformation and its intracellular distribution in a variety of cells and tissues
    • Yin, H., Albrecht, and J. H., Fattoum, A. 1981. Identification of gelsolin, a calcium-dependent regulatory protein of actin gel-sol transformation and its intracellular distribution in a variety of cells and tissues. J. Cell Biol. 91:901-906.
    • (1981) J. Cell Biol. , vol.91 , pp. 901-906
    • Yin, H.1    Albrecht2    J, H.3    Fattoum, A.4
  • 29
  • 32
    • 0023850804 scopus 로고
    • Severin, gelsolin and villin share a homologous sequence in regions presumed to contain F-actin severing domains
    • Andre, E., Lottspeich, F., Schleicher, M., and Noegel, A. 1988. Severin, gelsolin and villin share a homologous sequence in regions presumed to contain F-actin severing domains. J. Biol. Chem. 263:722-728.
    • (1988) J. Biol. Chem. , vol.263 , pp. 722-728
    • Andre, E.1    Lottspeich, F.2    Schleicher, M.3    Noegel, A.4
  • 33
    • 0023661298 scopus 로고
    • The F-actin capping proteins of Physarum polydephalum: Cap42(a) is very similar if not identical to fragmin and is structurally and functionally very homologous to gelsolin: cap42(b) is Phisarum actin
    • Ampe, C., and Vandekerchove, J. 1987. The F-actin capping proteins of Physarum polydephalum: cap42(a) is very similar if not identical to fragmin and is structurally and functionally very homologous to gelsolin: cap42(b) is Phisarum actin. EMBO J. 6:4149-4157.
    • (1987) EMBO J. , vol.6 , pp. 4149-4157
    • Ampe, C.1    Vandekerchove, J.2
  • 34
    • 0024293322 scopus 로고
    • Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats
    • Way, M., and Weeds, A. 1988. Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats. J. Mol. Biol. 203:1127-1133.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1127-1133
    • Way, M.1    Weeds, A.2
  • 35
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P. J., Gooch, J. T., Mannherz, H-G., and Weeds, A. G. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 36
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and alfa actinin: Implications for the requirements of severing and capping
    • Way, M., Pope, B. and Weeds, A. G. 1992. Evidence for functional homology in the F-actin binding domains of gelsolin and alfa actinin: implications for the requirements of severing and capping. J. Cell Biol. 119:835-842.
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 37
    • 0027014517 scopus 로고
    • Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis
    • Trifaró, J-M., Rodríguez Del Castillo, A., and Vitale, M. L. 1992. Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis. Mol. Neurobiol. 6:339-358.
    • (1992) Mol. Neurobiol. , vol.6 , pp. 339-358
    • Trifaró, J.-M.1    Rodríguez Del Castillo, A.2    Vitale, M.L.3
  • 38
    • 0026089715 scopus 로고
    • Two of the three actin binding domains of gelsolin bind to the same subdomain of actin
    • Pope, B., Way, M., and Weeds, A. G. 1991. Two of the three actin binding domains of gelsolin bind to the same subdomain of actin. FEBS Lett. 280:70-74.
    • (1991) FEBS Lett. , vol.280 , pp. 70-74
    • Pope, B.1    Way, M.2    Weeds, A.G.3
  • 39
    • 0025038549 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0
    • Huber, R., Schneider, M., Mayr, J., Römisch, J., and Paques, E. P. 1990. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution. FEBS Lett. 275:15-24.
    • (1990) Å Resolution. FEBS Lett. , vol.275 , pp. 15-24
    • Huber, R.1    Schneider, M.2    Mayr, J.3    Römisch, J.4    Paques, E.P.5
  • 40
    • 0023008203 scopus 로고
    • The actin filament severing domain of plasma gelsolin
    • Chaponnier, C., Janmey, P., and Yin, H. 1986. The actin filament severing domain of plasma gelsolin. J. Cell Biol. 103:1473-1481.
    • (1986) J. Cell Biol. , vol.103 , pp. 1473-1481
    • Chaponnier, C.1    Janmey, P.2    Yin, H.3
  • 41
    • 0023894120 scopus 로고
    • Gelsolin has 3 actin binding sites
    • Bryan, J. 1988. Gelsolin has 3 actin binding sites. J. Cell Biol. 106:1553-1562.
    • (1988) J. Cell Biol. , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 42
    • 0032488841 scopus 로고    scopus 로고
    • Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin
    • Marcu, M. G., Zhang, L., Elzagallaai, A., and Trifaró, J-M. 1998. Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. J. Biol. Chem. 273:3661-3668.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3661-3668
    • Marcu, M.G.1    Zhang, L.2    Elzagallaai, A.3    Trifaró, J.-M.4
  • 43
    • 0026945434 scopus 로고
    • 2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation
    • 2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation. J. Cell Biol. 119:797-810.
    • (1992) J. Cell Biol. , vol.119 , pp. 797-810
    • Rodríguez Del Castillo, A.1    Vitale, M.L.2    Trifaró, J.-M.3
  • 44
    • 0025337187 scopus 로고
    • Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids
    • Maekawa, S., and Sakai, H. 1990. Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids. J. Biol. Chem. 265:10940-10942.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10940-10942
    • Maekawa, S.1    Sakai, H.2
  • 45
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A., and Stossel, T. P. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 46
    • 0024403320 scopus 로고
    • Studies of inositol phospholipid-specific phospholipase C
    • Rhee, S. G., Suh, P. G., Ryu, S. H., and Sang, Y. L. 1989. Studies of inositol phospholipid-specific phospholipase C. Science 244:546-550.
    • (1989) Science , vol.244 , pp. 546-550
    • Rhee, S.G.1    Suh, P.G.2    Ryu, S.H.3    Sang, Y.L.4
  • 47
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequences in an actin monomer-binding domain of gelsolin
    • Yu, F-X, Sun, H-Q., Janmey, P. A., Yin, H. L. 1992. Identification of a polyphosphoinositide-binding sequences in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267:14616-14621.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.-X.1    Sun, H.-Q.2    Janmey, P.A.3    Yin, H.L.4
  • 48
    • 0026724890 scopus 로고
    • Phosphoinositide binding peptides derived from the sequences of gelsolin and villin
    • Janmey, P. A., Lamb, J., Allen, P. G., and Matsudaira, P. T. 1992. Phosphoinositide binding peptides derived from the sequences of gelsolin and villin. J. Biol. chem. 267:11818-11823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 50
    • 0030029849 scopus 로고    scopus 로고
    • Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate
    • Marcu, M. G., Zhang, L., Nau-Staudt, K., and Trifaró, J-M. 1996. Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate. Blood 87:20-24.
    • (1996) Blood , vol.87 , pp. 20-24
    • Marcu, M.G.1    Zhang, L.2    Nau-Staudt, K.3    Trifaró, J.-M.4
  • 51
    • 0018934798 scopus 로고
    • Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors
    • MacLean-Fletcher, S. D., and Pollard, T. D. 1980. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85:414-428.
    • (1980) J. Cell Biol. , vol.85 , pp. 414-428
    • MacLean-Fletcher, S.D.1    Pollard, T.D.2
  • 52
    • 0003353735 scopus 로고
    • Cuthbert, A. W. (ed..) Macmillan and Co. Ltd., London
    • Caldwell, P. C. 1970. Pages 10-16 in Cuthbert, A. W. (ed..) Calcium and Cellular Function. Macmillan and Co. Ltd., London.
    • (1970) Calcium and Cellular Function , pp. 10-16
    • Caldwell, P.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.